1.9.6.1: nitrate reductase (cytochrome)
This is an abbreviated version!
For detailed information about nitrate reductase (cytochrome), go to the full flat file.
Word Map on EC 1.9.6.1
-
1.9.6.1
-
nitrite
-
denitrification
-
denitrify
-
molybdenum
-
paracoccus
-
dissimilatory
-
denitrificans
-
n2o
-
pantotrophus
-
napf
-
nitrate-reducing
-
desulfuricans
-
molybdoenzymes
-
thiosphaera
-
cyma
-
fixk2
-
menaquinol
-
di-haem
-
bismolybdopterin
-
wolinella
-
high-g
-
narghi
-
norcbqd
-
nitrate-dependent
-
mo-containing
- 1.9.6.1
- nitrite
-
denitrification
-
denitrify
- molybdenum
- paracoccus
-
dissimilatory
- denitrificans
- n2o
- pantotrophus
- napf
-
nitrate-reducing
- desulfuricans
-
molybdoenzymes
-
thiosphaera
-
cyma
- fixk2
- menaquinol
-
di-haem
-
bismolybdopterin
-
wolinella
-
high-g
- narghi
-
norcbqd
-
nitrate-dependent
-
mo-containing
Reaction
2 ferrocytochrome
+
2 H+
+
Synonyms
benzyl viologen-nitrate reductase, EC 1.7.99.4, mmol_1648, More, NAP, NAP enzyme, Nap-alpha, NAP-beta, NapA, napA-beta, NapAB, NapABC, NapDAGHB, NapEDABC, nitrate reductase, periplasmic, periplasmic nitrate reductase, periplasmic nitrate reductases, reductase, nitrate (cytochrome), respiratory nitrate reductase, single subunit Nap-type periplasmic nitrate reductase
ECTree
1.9.6.1 nitrate reductase (cytochrome)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.9.6.1 - nitrate reductase (cytochrome)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nitrate + reduced acceptor
nitrite + oxidized acceptor
-
-
-
-
?
nitrate + reduced benzyl viologen
nitrite + oxidized benzyl viologen
-
-
-
?
nitrate + reduced methyl viologen
nitrite + oxidized methyl viologen
-
-
-
-
?
nitrite + methyl viologen
nitrate + oxidized methyl viologen
-
-
-
-
?
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
Cereibacter sphaeroides DSM 158
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
-
-
-
?
2 ferrocytochrome + 2 H+ + nitrate
2 ferricytochrome + nitrite
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
?
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
-
-
-
?
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
-
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
Shewanella oneidensis MR-1 / ATCC 700550
-
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
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
-
-
-
?
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
?
-
Cereibacter sphaeroides DSM 158
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
?
-
Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1
-
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
-
-
?
