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2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
-
-
-
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism. The second sphere type of mechanism is supported by the recent X-ray structures of Nap from Desulfovibrio desulf uricans ATCC 27774 and Cupriavidus necator H16, in which the sixth sulfur ligand of the Mo interacts with the sulfur from the cysteine residue and generates a bidentate persulfido ligand that sterically blocks the access of the substrate to the Mo ion, modelling
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
-
2 ferrocytochrome + 2 H+ + nitrate = 2 ferricytochrome + nitrite + H2O
sulfur-shift mechanism catalytic mechanism, detailed overview. The mechanism is defined by a change in the Mo ion coordination, which involves a first-to-second shell displacement (shift) of the sulfur from the Cys, resulting in a free coordination position that is used by the enzyme to bind the substrate with a low energy cost, molybdenum coordinates an oxygen atom from the substrate, an oxygen atom from the substrate is transferred to the Mo ion, and later released as a water molecule. The reaction requires two electrons, which are provided by external reducing species, and two protons that are obtained from the solvent either directly or indirectly mediated by residues from the enzyme catalytic pocket
-
-
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2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
2 reduced methyl viologen + 2 H+ + nitrate
2 oxidized methyl viologen + nitrite
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
nitrate + reduced acceptor
nitrite + acceptor
nitrate + reduced acceptor
nitrite + oxidized acceptor
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
nitrite + methyl viologen
nitrate + oxidized methyl viologen
-
-
-
-
?
additional information
?
-
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 reduced methyl viologen + 2 H+ + nitrate
2 oxidized methyl viologen + nitrite
artificial electron acceptor
-
-
r
2 reduced methyl viologen + 2 H+ + nitrate
2 oxidized methyl viologen + nitrite
artificial electron acceptor
-
-
r
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the periplasmic cytochrome c-linked nitrate reductase is encoded by the napFDAGHBC operon. The napF operon apparently encodes a low-substrate-induced reductase that is maximally expressed only at low levels of nitrate. Expression is suppressed under high-nitrate conditions. In contrast, the narGHJI operon is only weakly expressed at low nitrate levels but is maximally expressed when nitrate is elevated. The narGHJI operon is therefore a high-substrate-induced operon that somehow provides a second and distinct role in nitrate metabolism by the cell. Nitrite, the end product of each enzyme, has only a minor effect on the expression of either operon. Finally, nitrate, but not nitrite, is essential for repression of napF gene expression. These studies reveal that nitrate rather than nitrite is the primary signal that controls the expression of these two nitrate reductase operons in a differential and complementary fashion
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
periplasmic nitrate reductase is expressed under nitrate-limiting conditions. NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via cytochrome NapC and NapB to NapA
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinoneubiquinol couple via cytochrome NapC and NapB to NapA
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
-
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the reduction of nitrate catalysed by NAP takes place in the 90 kDa NapA subunit
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
reduced benzyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
reduced methyl viologen as electron donor
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
the enzymes EC 1.7.99.4 and EC 1.9.6.1 are probably identical, in vivo cytochrome serves as electron donor in the electron transport chain to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
electron transport chain in vivo: Fe3 + via specific cytochrome-nitrate reductase to NO3-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen + H2O
-
very high substrate specificity. The enzyme does not reduce any other oxocompound (chlorate, bromate, iodate, nitrite, molybdate, sulphate, thiosulphate, tetrathionate, selenate, dimethyl sulphoxide, trimethylamine-A-oxide, borate and arsenate)
-
-
?
additional information
?
-
-
the enzymes EC 1.7.99.4 and EC 1.9.6.1 are probably identical, in vivo cytochrome serves as electron donor in the electron transport chain to nitrate
-
-
?
additional information
?
-
-
the nap operon encodes the only nitrate reductase in Campylobacter jejuni and that it is essential in mediating growth using nitrate as a terminal electron acceptor under oxygen-limited conditions
-
-
?
additional information
?
-
the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation
-
-
?
additional information
?
-
the MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation
-
-
?
additional information
?
-
-
an insertion in the napA gene leads to a complete loss of enzyme activity but does not abolish the ability of Alcaligenes eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration. Nevertheless, the NAP-deficient mutant shows delayed growth after transition from aerobic to anaerobic respiration, suggesting a role for periplasmic nitrate reductase in the adaptation to anaerobic metabolism
-
-
?
additional information
?
-
-
an insertion in the napA gene leads to a complete loss of enzyme activity but does not abolish the ability of Alcaligenes eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration. Nevertheless, the NAP-deficient mutant shows delayed growth after transition from aerobic to anaerobic respiration, suggesting a role for periplasmic nitrate reductase in the adaptation to anaerobic metabolism
-
-
?
additional information
?
-
-
NapABC enzyme is responsible for nitrate dissimilation. Periplasmic nitrate reductase (NapABC enzyme) can function in anaerobic respiration but does not constitute a site for generating proton motive force. napF-lacZ is expressed preferentially at relatively low nitrate concentrations in continuous cultures. This finding support the hypothesis that NapABC enzyme may function in Escherichia coli when low nitrate concentrations limit the bioenergetic efficiency of nitrate respiration via NarGHI enzyme
-
-
?
additional information
?
-
-
NapAB catalysed nitrate reduction driven by direct electron transfer from the electrode to NapAB, protein film voltammetry. Exploration of the nitrate reductase activity of purified NapAB as a function of electrochemical potential, substrate concentration and pH using protein film voltammetry. Nitrate reduction by NapAB occurs at potentials below approx. 0.1 V at pH 7. These are lower potentials than required for NarGH nitrate reduction. The potentials required for Nap nitrate reduction are also likely to require ubiquinol/ubiquinone ratios higher than are needed to activate the H+-pumping oxidases expressed during aerobic growth where Nap levels are maximal. Thus the operational potentials of Paracoccus pantotrophus NapAB are consistent with a productive role in redox balancing
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
nitrate + reduced acceptor
nitrite + acceptor
additional information
?
-
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
r
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
the periplasmic cytochrome c-linked nitrate reductase is encoded by the napFDAGHBC operon. The napF operon apparently encodes a low-substrate-induced reductase that is maximally expressed only at low levels of nitrate. Expression is suppressed under high-nitrate conditions. In contrast, the narGHJI operon is only weakly expressed at low nitrate levels but is maximally expressed when nitrate is elevated. The narGHJI operon is therefore a high-substrate-induced operon that somehow provides a second and distinct role in nitrate metabolism by the cell. Nitrite, the end product of each enzyme, has only a minor effect on the expression of either operon. Finally, nitrate, but not nitrite, is essential for repression of napF gene expression. These studies reveal that nitrate rather than nitrite is the primary signal that controls the expression of these two nitrate reductase operons in a differential and complementary fashion
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
NapG and H, but not NapF, are essential for electron transfer from ubiquinol to NapAB. NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB. It is proposed that NapG and H form an energy conserving quinol dehydrogenase functioning as either components of a proton pump or in a Q cycle, as electrons are transferred from ubiquinol to the membrane-bound cytochrome NapC
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
periplasmic nitrate reductase is expressed under nitrate-limiting conditions. NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via cytochrome NapC and NapB to NapA
-
-
?
nitrate + ferrocytochrome
nitrite + ferricytochrome + H2O
-
-
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
the enzymes EC 1.7.99.4 and EC 1.9.6.1 are probably identical, in vivo cytochrome serves as electron donor in the electron transport chain to nitrate
-
-
?
nitrate + reduced acceptor
nitrite + acceptor
-
electron transport chain in vivo: Fe3 + via specific cytochrome-nitrate reductase to NO3-
-
-
?
additional information
?
-
-
the nap operon encodes the only nitrate reductase in Campylobacter jejuni and that it is essential in mediating growth using nitrate as a terminal electron acceptor under oxygen-limited conditions
-
-
?
additional information
?
-
-
an insertion in the napA gene leads to a complete loss of enzyme activity but does not abolish the ability of Alcaligenes eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration. Nevertheless, the NAP-deficient mutant shows delayed growth after transition from aerobic to anaerobic respiration, suggesting a role for periplasmic nitrate reductase in the adaptation to anaerobic metabolism
-
-
?
additional information
?
-
-
an insertion in the napA gene leads to a complete loss of enzyme activity but does not abolish the ability of Alcaligenes eutrophus to use nitrate as a nitrogen source or as an electron acceptor in anaerobic respiration. Nevertheless, the NAP-deficient mutant shows delayed growth after transition from aerobic to anaerobic respiration, suggesting a role for periplasmic nitrate reductase in the adaptation to anaerobic metabolism
-
-
?
additional information
?
-
-
NapABC enzyme is responsible for nitrate dissimilation. Periplasmic nitrate reductase (NapABC enzyme) can function in anaerobic respiration but does not constitute a site for generating proton motive force. napF-lacZ is expressed preferentially at relatively low nitrate concentrations in continuous cultures. This finding support the hypothesis that NapABC enzyme may function in Escherichia coli when low nitrate concentrations limit the bioenergetic efficiency of nitrate respiration via NarGHI enzyme
-
-
?
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bis(molybdopterin guanine dinucleotide)molybdenum cofactor
cytochrome c552
-
the enzyme is a complex of a 93000 Da polypeptide and a 16000 Da nitrate-oxidizable cytochrome c552, cytochrome c552 contains two c-type heme moieties
-
additional information
-
enzyme contains no flavin
-
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
4Fe-4S-center
-
the 90 kDa NapA subunit contains a one [4Fe-4S] iron-sulfur cluster
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
NapA contains a molybdo-bis(molybdopterin guanine dinucleotide) cofactor
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
subunit NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster
cytochrome
-
presence of a bound cytochrome
-
cytochrome
-
NapG and NapH form a quinol dehydrogenase that couples electron transfer from the high midpoint redox potential ubiquinone-ubiquinol couple via cytochrome NapC and NapB to NapA
-
cytochrome
-
the membrane-bound cytochrome NapC is essential for electron transfer from both ubiquinol and menaquinol to NapAB
-
cytochrome c
-
-
cytochrome c
di-heme cytochrome c redox partner, NapB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
i.e. NapB, contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from enzyme NapA. Once in the periplasm they form the heterodimer NapAB
cytochrome c
two surface-exposed c-type hemes, NapB
heme
-
contains 1.3 mol heme per mol of protein (assuminga 110-kDa molecular mass)
heme
subunit NapB is a diheme cytochrome c
heme
-
the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB)
heme
a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor
molybdenum cofactor
-
-
molybdenum cofactor
a Mo-pyranopterin cofactor
molybdenum cofactor
i.e. MoCo, the EPR signature of the MoCo is heterogeneous. The MoCo in Rhodobacter sphaeroides periplasmic nitrate reductase (NapAB) is subject to a slow, irreversible reductive activation. The inactive form features an open, oxidized pyranopterin, which is closed upon reduction. Distict from that, a slow, reversible inactivation/reactivation process occurs at high nitrate concentration, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdenum cofactor
synthesis of the Mo-pyranopterin cofactor, overview
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
molybdopterin
-
the 90 kDa NapA subunit contains a Mo-bis-molybdopterin guanine dinucleotide cofactor
[4Fe-4S] cluster
-
-
[4Fe-4S] cluster
in close proximity to the MoCo
[4Fe-4S]-center
-
[4Fe-4S]-center
a [4Fe-4S] cluster and two c-type hemes form an intramolecular electron transfer chain that deliver electrons to the active site. Residue lysine 56 connects, through hydrogen-bonds, the [4Fe-4S] center to one of the pyranopterin ligands of the Mo-cofactor
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evolution
genotyping of different strains from M and G populations, overview. The only mutated gene shared between the strains from populations M and G is bll4572, this gene is mutated in all six strains
evolution
periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans and formate dehydrogenase (Fdh) from Escherichia coli K-12, both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the enzyme belongs to the DMSO reductase family
evolution
the periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans belongs to the DMSO reductase family, subfamily I. Classification of Mo-pyranopterin dependent enzymes from the DMSO reductase family, e.g. periplasmic nitrate reductase and formate dehydrogenase, overview. Comparison of the sulfur-shift mechanism in nitrate reductase (Nap) and in formate dehydrogenase (Fdh), detailed overview
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
-
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
-
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
-
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
evolution
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) from Desulfovibrio desulfuricans and formate dehydrogenase (Fdh) from Escherichia coli K-12, both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
evolution
-
genotyping of different strains from M and G populations, overview. The only mutated gene shared between the strains from populations M and G is bll4572, this gene is mutated in all six strains
-
evolution
-
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) belongs to the DMSO reductase family, subfamily I
-
evolution
-
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
-
evolution
-
the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
-
evolution
-
the enzyme belongs to the DMSO reductase family
-
evolution
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the prokaryotic nitrate reductases can be subgrouped as respiratory nitrate reductases (Nar), assimilatory nitrate reductases (Nas), and periplasmic nitrate reductases (Nap). Periplasmic nitrate reductase (Nap) and formate dehydrogenase (Fdh), both belonging to the DMSO reductase family, subfamily I, have a very similar structure, but very different activities. The show key differences that tune them for completely different functions in living cells. Both enzymes share almost identical three-dimensional protein foldings and active sites, in terms of coordination number, geometry and nature of the ligands. The substrates of both enzymes (nitrate and formate) are polyatomic anions that also share similar charge and stereochemistry. In terms of the catalytic mechanism, both enzymes have a common activation mechanism (the sulfur-shift mechanism) that ensures a constant coordination number around the metal ion during the catalytic cycle. In spite of these similarities, they catalyze very different reactions: Nap abstracts an oxygen atom from nitrate releasing nitrite, whereas FdH catalyzes a hydrogen atom transfer from formate and releases carbon dioxide. Detailed comparison, overview. A key difference between the catalytic mechanisms of Nap and FdH is the fact that only Mo is used to reduce nitrate but in Fdhs both Mo and W are catalytically competent to oxidize formate to carbon dioxide
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malfunction
a gene nap deletion mutant can no longer grow on methanol in contrast to the wild-type and shows almost abolished N2O production from nitrate
malfunction
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Salmonella enterica serovar Typhimurium strains with defects in either nitrate reductase A (narG mutant) or the regulator inducing its transcription in the presence of high concentrations of nitrate (narL mutant) exhibit growth comparable to that of wild-type Salmonella enterica serovar Typhimurium. In contrast, a strain lacking a functional periplasmic nitrate reductase (napA mutant) exhibits a marked growth defect in the lumen of the colon. Inactivation of narP, encoding a response regulator that activates napABC transcription in response to low nitrate concentrations, significantly reduces the growth of Salmonella enterica serovar Typhimurium in the murine host gut lumen
malfunction
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Salmonella enterica serovar Typhimurium strains with defects in either nitrate reductase A (narG mutant) or the regulator inducing its transcription in the presence of high concentrations of nitrate (narL mutant) exhibit growth comparable to that of wild-type Salmonella enterica serovar Typhimurium. In contrast, a strain lacking a functional periplasmic nitrate reductase (napA mutant) exhibits a marked growth defect in the lumen of the colon. Inactivation of narP, encoding a response regulator that activates napABC transcription in response to low nitrate concentrations, significantly reduces the growth of Salmonella enterica serovar Typhimurium in the murine host gut lumen
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malfunction
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a gene nap deletion mutant can no longer grow on methanol in contrast to the wild-type and shows almost abolished N2O production from nitrate
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metabolism
cytochromes c encoded by genes in close proximity to the genes for XoxF proteins and methylamine dehydrogenase functions are likely involved in the metabolism with Nap, pathway overview
metabolism
NasST regulates the nitrate-mediated response of nosZ and napE genes, from the dissimilatory denitrification pathway, regulation of nos and nap genes by the NasST system in the absence of nitrate in mutant strains, overview
metabolism
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NasST regulates the nitrate-mediated response of nosZ and napE genes, from the dissimilatory denitrification pathway, regulation of nos and nap genes by the NasST system in the absence of nitrate in mutant strains, overview
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metabolism
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cytochromes c encoded by genes in close proximity to the genes for XoxF proteins and methylamine dehydrogenase functions are likely involved in the metabolism with Nap, pathway overview
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physiological function
the Nap-deficient mutant KD102 shows increased diauxic lag when switched from aerobic to anoxic respiration, suggesting Nap is responsible for shorter lags and helps in adaptation to anoxic metabolism after transition from aerobic conditions
physiological function
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napAB expression is required for anaerobic growth recovery by DELTAnarXL (a deletion encompassing the bulk of narXL)
physiological function
Escherichia coli is a Gram-negative bacterium that can use nitrate during anaerobic respiration. The catalytic subunit of the involved periplasmic nitrate reductase NapA contains two types of redox cofactor and is exported across the cytoplasmic membrane by the twin-arginine protein transport pathway
physiological function
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Salmonella enterica serovar Typhimurium uses the periplasmic nitrate reductase to support its growth on the low nitrate concentrations encountered in the gut, a strategy that may be shared with other enteric pathogens
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap enzyme from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the Nap enzyme from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
physiological function
the single subunit nitrate reductase (Nap) appears to be involved in both the assimilatory and the dissimilatory denitrification pathways. The role in the former is supported by the methanol growth deficiency of the mutant when nitrate is used as a nitrogen source, and the role in the latter is supported by the lack of accumulation of N2O in the mutant
physiological function
a mutant strain defective for napA is not able to denitrify and grow on nitrate. The wild-type strain reaches 40 000 ppm of N2O emission and its growth is 10fold higher than that of the mutant strain. In the presence of nitrite as terminal electron acceptor, both wild-type and mutant are able to denitrify and to grow with no significant difference between both strains. NapA plays a role in Agrobacterium fabrum C58 fitness but is not involved in A. fabrum C58 root colonization
physiological function
the anaerobic reduction of NO3- to N2O is lower in Bradyrhizobium japonicum than in Bradyrhizobium diazoefficiens due to impaired periplasmic nitrate reductase (Nap) activity in B. japonicum. Impaired Nap activity in B. japonicum is due to low Nap protein levels
physiological function
the anaerobic reduction of NO3- to N2O is lower in Bradyrhizobium japonicum than in Bradyrhizobium diazoefficiens due to impaired periplasmic nitrate reductase (Nap) activity in B. japonicum. Impaired Nap activity in B. japonicum is due to low Nap protein levels
physiological function
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the anaerobic reduction of NO3- to N2O is lower in Bradyrhizobium japonicum than in Bradyrhizobium diazoefficiens due to impaired periplasmic nitrate reductase (Nap) activity in B. japonicum. Impaired Nap activity in B. japonicum is due to low Nap protein levels
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physiological function
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a mutant strain defective for napA is not able to denitrify and grow on nitrate. The wild-type strain reaches 40 000 ppm of N2O emission and its growth is 10fold higher than that of the mutant strain. In the presence of nitrite as terminal electron acceptor, both wild-type and mutant are able to denitrify and to grow with no significant difference between both strains. NapA plays a role in Agrobacterium fabrum C58 fitness but is not involved in A. fabrum C58 root colonization
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physiological function
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the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
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physiological function
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Salmonella enterica serovar Typhimurium uses the periplasmic nitrate reductase to support its growth on the low nitrate concentrations encountered in the gut, a strategy that may be shared with other enteric pathogens
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physiological function
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the single subunit nitrate reductase (Nap) appears to be involved in both the assimilatory and the dissimilatory denitrification pathways. The role in the former is supported by the methanol growth deficiency of the mutant when nitrate is used as a nitrogen source, and the role in the latter is supported by the lack of accumulation of N2O in the mutant
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physiological function
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the Nap enzyme from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source
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additional information
modeling of regulation of nap and nos genes by NasST system in Bradyrhizobium japonicum strain USDA110 and nasS and Nos++ mutant strains
additional information
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modeling of regulation of nap and nos genes by NasST system in Bradyrhizobium japonicum strain USDA110 and nasS and Nos++ mutant strains
additional information
NapD is a small cytoplasmic protein that is essential for the activity of the periplasmic nitrate reductase and binds tightly to the twinarginine signal peptide of NapA. NapA is structured in its unbound form. The NapA signal peptide undergoes conformational rearrangement upon interaction with NapD. NapA is at least partially folded when bound by its NapD partner. The NapD chaperone binds primarily at the NapA signal peptide in this system and points towards a role for NapD in the insertion of the molybdenum cofactor
additional information
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NapD is a small cytoplasmic protein that is essential for the activity of the periplasmic nitrate reductase and binds tightly to the twinarginine signal peptide of NapA. NapA is structured in its unbound form. The NapA signal peptide undergoes conformational rearrangement upon interaction with NapD. NapA is at least partially folded when bound by its NapD partner. The NapD chaperone binds primarily at the NapA signal peptide in this system and points towards a role for NapD in the insertion of the molybdenum cofactor
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure, structure overview. Above the region of the metal center, the enzyme presents an arginine residue, Arg354,that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, Arg354,that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA, product of the napA gene, is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bis-PGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Paracoccus pantotrophus catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. But the Nap from Pseudomonas sp. G-179 lacks these two genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Rhodobacter sphaeroides catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Shewanella gelidimarina catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
additional information
the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In bacteria like Desulfovibrio desulfuricans ATCC 27774 and Escherichia coli K12, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present
additional information
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the Salmonella enterica serovar Typhimurium genome contains three nitrate reductases, encoded by the narGHI, narZYV, and napABC genes
additional information
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modeling of regulation of nap and nos genes by NasST system in Bradyrhizobium japonicum strain USDA110 and nasS and Nos++ mutant strains
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additional information
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the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Cupriavidus necator catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
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additional information
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the Salmonella enterica serovar Typhimurium genome contains three nitrate reductases, encoded by the narGHI, narZYV, and napABC genes
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additional information
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the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bisPGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (Twin Arginine Translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. But the Nap from Pseudomonas sp. G-179 lacks these two genes
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additional information
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the enzyme shows a sulfur-shift mechanism catalytic mechanism, the active site is deeply buried and centered on the Mo atom, which is hexacoordinated to four sulfur atoms of two pyranopterin guanosine dinucleotides, one inorganic sulfur, and one S (Nap) atom from the side chain of a Cys, structure. Above the region of the metal center, the enzyme presents an arginine residue, that is proposed to be key for stabilization and substrate binding. The side chain of this residues probably interacts electrostatically with the substrates, compensating for the negative charge and favoring their interaction with the negatively charged active site. Comparisons of reaction mechanisms of members of the DMSO reductase family and structure analysis and modelling, overview. The NapA (product of the napA gene) is the catalytic subunit that contains the Mo-bis-PGD and one 4Fe-4S center involved in electron transfer. Similar to other periplasmic Mo- and W-enzymes, immature NapA contains a signal peptide that is recognized by the TAT (twin arginine translocator) system. Prior to translocation, the two metallic cofactors are incorporated into NapA with the aid of the chaperone NapD, which accompanies the assembled metalloenzyme to the transporter, maturation mechanism of Mo. NapB contains two c-type hemes and is assembled and secreted into the periplasm by the Ccm (cytochrome c maturation) machinery independently from NapA. Once in the periplasm they form the heterodimer NapAB, except in the case of monomeric Naps. It is remarkable that napM is present only when the napB gene is absent. NapM is a tetrahemic c-type cytochrome. This cytochrome may mediate electron transfer to NapA in a similar way that NapB does in heterodimeric Naps. NapC is a membrane-anchored protein harboring four c-type hemes belonging to the NapC/NirT family. In some bacteria, where nitrate reduction catalyzed by Nap is coupled to an energy conserving process, the genes napG and napH are always present. Nap from Paracoccus pantotrophus catalyzes nitrate reduction to consume the excess of reducing equivalents generated by consumption of the carbon source, which is in agreement with the lack of napG and napH genes
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dimer
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1 * 93000 + 1 * 16000, SDS-PAGE
?
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x * 90000 + x * 16000, two-subunit complex, NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster. NapB is an 16000 Da electron-transfer subunit, which in other bacteria binds two c-type haems
?
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1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively
?
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x * 16000 + x * 90000, SDS-PAGE
heterodimer
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heterodimer
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1 * 17000 + 1 * 87000, SDS-PAGE
heterodimer
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1 * 93309 + 1 * 18924, calculated from sequence
heterodimer
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1 * 17000 + 1 * 87000, SDS-PAGE
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heterodimer
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1 * 93309 + 1 * 18924, calculated from sequence
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heterodimer
1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
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the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
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the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
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additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
-
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
PELDOR analysis of recombinant MTSL-labelled MalE-NapASP fusion mutant S4C/S24C alone or in complex with NapD, comparison of bound, NMR-derived NapASP helix from PDB ID 2PQ4 versus free generated helix, positions of the spin labels in the two conformations of the signal peptide, overview
additional information
-
PELDOR analysis of recombinant MTSL-labelled MalE-NapASP fusion mutant S4C/S24C alone or in complex with NapD, comparison of bound, NMR-derived NapASP helix from PDB ID 2PQ4 versus free generated helix, positions of the spin labels in the two conformations of the signal peptide, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the nap operon of Escherichia coli K-12, encoding a periplasmic nitrate reductase, encodes seven proteins. The catalytic complex in the periplasm, NapANapB receives electrons from the quinol pool via the membrane-bound cytochrome NapC. Like NapA, B and C, NapD, is also essential for Nap activity. None of the remaining three polypeptides, NapF, G and H, which are predicted to encode non-heme, iron-sulfur proteins, are essential for Nap activity
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
-
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
-
additional information
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
additional information
-
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview
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