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Mo
-
0.0025 mmol Mo per g protein
selenium
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[NiFeSe]-hydrogenase
additional information
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no increase in the hydrogenase activity is observed in response to ferric sulfate, ferric citrate, ferric ammonium citrate, and ferric nitrate
CN-
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the auxiliary proteins HoxL and HoxV assist in assembly of the Fe(CN-)2CO moiety
CN-
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the catalytic center is equipped with 1.8 CN- per protein molecule
CN-
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contains two CN- molecules at the active site
CO
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the auxiliary proteins HoxL and HoxV assist in assembly of the Fe(CN-)2CO moiety
CO
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the catalytic center is equipped with one CO
Fe
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0.134 mmol Fe per g protein
Fe
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uptake [NiFe] hydrogenase
Fe
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contains bimetallic center in active site
Fe
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contains Fe-s clusters
Fe
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enzyme contains Ni-Fe center and Fe-S clusters
Fe
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Ni-Fe active site. Presence of eight Fe-S clusters, three [2Fe-2S] clusters and five [4Fe-4S] clusters
Fe
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HydADELTAEFG binds a [4Fe-4S] cluster
Fe
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lacks the ferredoxin-like clusters, but contains the H-cluster [Fe4S4] component
Fe
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the HydA1 H-cluster consists of a [4Fe4S] cluster and a diiron site, 2FeH
Fe
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iron-sulfur cluster as well as 4Fe-4S-ferredoxin-type cluster
Fe
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the large subunit HoxC is purified without its small subunit. Two forms of HoxC are identified. Both forms contain iron but only substoichiometric amounts of nickel. One form is a homodimer of HoxC whereas the second also contains the NiFe site maturation proteins HypC and HypB. Despite the presence of the NiFe active site in some of the proteins, both forms, which lack the FeS clusters normally present in hydrogenases, cannot activate hydrogen. The incomplete insertion of nickel into the NiFe site provides direct evidence that Fe precedes Ni in the course of metal center assembly
Fe
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is composed of a small subunit, capable in coordinating one [3Fe4S] and two [4Fe4S] clusters
Fe
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the auxiliary proteins HoxL and HoxV assist in assembly of the Fe(CN-)2CO moiety
Fe
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[NiFeSe]-hydrogenase, absence of a [3Fe-4S] cluster
Fe
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contains several [4Fe-4S] clusters
Fe
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3Fe-xS and 4Fe-4S clusters
Fe
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14 atoms per molecule, 2 4Fe-4S clusters
Fe
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[FeFe]-hydrogenase.The H cluster (hydrogen-activating cluster) contains a di-iron centre ([2Fe]H subcluster, a (L)(CO)(CN)Fe(mu-RS2)(mu-CO)Fe (CysS)(CO)(CN) group) covalently attached to a cubane iron-sulphur cluster ([4Fe-4S]H subcluster). The added redox equivalent not only affects the [4Fe-4S]H subcluster, but also the di-iron centre
Fe
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11 atoms per mol enzyme
Fe
-
10.6 atoms per mol enzyme
Fe
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iron-sulfur cluster as well as 4Fe-4S-ferredoxin-type cluster
Fe
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contains several [4Fe-4S] clusters
Fe
-
hydrogen bonding affects the [NiFe] active site
Fe
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specific protein-protein interactions of maturation proteins may be required during [FeFe] cluster synthesis and/or insertion. Maturation proteins HydE and HydG interact with the [FeFe] hydrogenase large subunit HydA, which binds the H-cluster. Neither HydE nor HydG interact with the [FeFe] hydrogenase small subunit, HydB. No interaction of HydF, which catalyzes an energy-dependent step during H-cluster assembly or insertion, with either HydA or HydB
Fe
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the Hred form is assigned as a mixture of an Fe(I)Fe(I) form with an open site on the distal iron center and either a Fe(I)Fe(I) form in which the distal cyanide is protonated or a Fe(II)Fe(II) form with a bridging hydride ligand. The Hox form is assigned as a valence-localized Fe(I)Fe(II) redox level with an open site at the distal iron. The Hox air form is assigned as an Fe(II)Fe(II) redox level with OH- or OOH- bound to the distal iron center that may or may not have an oxygen atom bound to one of the sulfur atoms of the dithiolate linker
Fe
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two ferredoxin-like [Fe4S4] clusters
Fe
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the Hred form is assigned as a mixture of an Fe(I)Fe(I) form with an open site on the distal iron center and either a Fe(I)Fe(I) form in which the distal cyanide is protonated or a Fe(II)Fe(II) form with a bridging hydride ligand. The Hox form is assigned as a valence-localized Fe(I)Fe(II) redox level with an open site at the distal iron. The Hox air form is assigned as an Fe(II)Fe(II) redox level with OH- or OOH- bound to the distal iron center that may or may not have an oxygen atom bound to one of the sulfur atoms of the dithiolate linker
Fe
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12.2 mol per mol enzyme, iron-sulfur protein
Fe
-
10.9 mol per tetramer, 3Fe-4S cluster
Fe
-
membrane-bound [NiFe]-hydrogenase exhibits prominent electron paramagnetic resonance signals originating from [3Fe4S]1 and [4Fe4S]1 clusters
Fe
Megalodesulfovibrio gigas
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Fe
Megalodesulfovibrio gigas
NiFe-hydrogenase
Fe
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iron-sulfur cluster as well as 4Fe-4S-ferredoxin-type cluster
Fe
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iron center octahedrally coordinated by one dithiothreitol-sulfur and one dithiothreitol-oxygen, two CO, the nitrogen of 2-pyridinol and the 6-formylmethyl group of 2-pyridinol in an acyliron ligation
Fe
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11.3 mol per mol of enzyme
Fe
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21 atoms per mol enzyme, 5 4Fe-4S cluster and 1 2Fe-2S cluster
Fe
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31 g iron per 185 g enzyme
Fe
Solidesulfovibrio fructosivorans
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contains FeNi-center
Fe
Solidesulfovibrio fructosivorans
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contains Ni-Fe bimetallic center as active site
Fe
Solidesulfovibrio fructosivorans
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contains several [4Fe-4S] clusters
Fe
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iron azadithiolate phosphine-substituted complex and its protonated species featuring the NH proton and/or bridging Fe hydride, [Fe2(micro-S(CH2)2NnPr(H)m(CH2)2S)(micro-H)n(CO)4(PMe3)2]2 (2m+2n)+, mimic the active site of Fe-only hydrogenase. The ability to accept protons for the aza nitrogen and the Fe sites is essential for the enzymatic H2 production at the mild potential
Fe
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protonation can take place in a terminal fashion at a single Fe or by bridging between two iron centres, protonation of a model of the subsite of [FeFe]-hydrogenase, [Fe2(m-pdt)(CO)4(PMe3)2], occurs via a two-step mechanism
Fe
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protonation of diiron dithiolato complexes can occur at a single Fe site, even for symmetrical (FeI)2 compounds. The terminal hydride [HFe2(S2C3H6)(CO)2(dppv)2]+ catalyzes proton reduction at potentials 200 mV milder than the isomeric bridging hydride, thereby establishing a thermodynamic advantage for catalysis operating via terminal hydride
Fe
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the Fe(CO)2(Pi-Pr3) site is rotated in solution, driven by steric factors. Fe atom featuring a vacant apical coordination position is an electrophilic Fe(I) center. One-electron oxidation of [Fe2(S2C2H4)(CN)(CO)3(dppv)]- results in 2e oxidation of 0.5 equiv to give the micro-cyano derivative [FeI2(S2C2H4)(CO)3(dppv)](micro-CN)[FeII2(S2C2H4)(micro-CO)(CO)2(CN)(dppv)]
Fe
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has Fe-S clusters, contains 10 g atoms of Fe per mol of protein
Fe
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7-8 atoms per mol enzyme, 3Fe-4S cluster
Fe
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contains several [4Fe-S] and [2Fe-2S] cluster
Fe
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the electron acceptor interacts only with the [FeS]distal cluster in the hydrogenase, and accordingly the autocatalyst is a hydrogenase form in which the [FeS]distal cluster holds an electron (i.e., at least the [FeS]distal cluster is reduced)
Fe
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4Fe-4S and 2Fe-2S clusters
Fe2+
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essential element for the assembly and maturation, the addition of Fe-EDTA (0.05 mM) does not affect the level of hydrogenase activity
Fe2+
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1 mM increases hydrogenase activity 4fold, is not sufficient to increase hydrogenase activities without S-adenosyl methionine and the standard 20 L-amino acids
Fe2+
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contains a Fe2+-binding site
Fe2+
Megalodesulfovibrio gigas
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the active site has a characteristic bis(micro-thiolato)NiFe unit, where the Ni atom and the Fe atom are bridged by an undetermined oxygen-bearing ligand. This ligand probably derives from the aqueous solvent and is therefore most likely to be H2O, OH- or O2-. A NiFe complex is not able to activate H2 when coordinated with an CH3CN ligand, thus a highly labile ligand that is simultaneously able to act as a Lewis base for the heterolytic activation of H2 is crucial to the action of H2ase. The CH3CN-coordinated Ni(II)Fe(II) complex is unstable in the presence of water and decomposed to the Ni(II) complex and the Fe(II) complex via the Fe-S bond cleavage in water. In order to synthesise H2O-coordinated NiFe complexes in aqueous media, the Lewis acidity of the Fe centre must be increased to form strong Fe-S bonds. Thus, organometallic ligands with a back-donating character to form Fe-C bonds are required
Iron
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within the catalytic centre one carbonyl and two cyanide ligands are covalently attached to the iron
Iron
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the enzyme harbors an iron-containing cofactor, in which a lowspin iron is complexed by a pyridone, two CO and a cysteine sulfur, [Fe] hydrogenase apoenzyme is converted completely into [Fe] hydrogenase holoenzyme by mixing the apoenzyme with a 3fold excess of the iron-containing [Fe] hydrogenase cofactor
Iron
contains 0.23 Fe atoms per molecule of large subunit HyhL
Ni
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0.0025 mmol Ni per g protein
Ni
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uptake [NiFe] hydrogenase
Ni
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0.725 mol per enzyme
Ni
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contains bimetallic center in active site
Ni
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enzyme contains Ni-Fe center
Ni
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contains Ni in the catalytic center
Ni
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0.9 atoms per mol enzyme
Ni
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0.9 atoms per mol enzyme
Ni
-
hydrogen bonding affects the [NiFe] active site
Ni
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[NiFe] hydrogenase has two different oxidized states, Ni-A (unready, exhibits a lag phase in reductive activation) and Ni-B (ready). Ni-B possesses a monatomic nonprotein bridging ligand at the Ni-Fe active site, whereas Ni-A has a diatomic species
Ni
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1.06 mol per tetramer
Ni
Megalodesulfovibrio gigas
-
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Ni
Megalodesulfovibrio gigas
NiFe-hyrogenase
Ni
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0.9 mol per mol of enzyme
Ni
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0.9 atoms per mol enzyme
Ni
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31 g nickel per 185 g enzyme
Ni
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Rhizobium leguminosarum biovar viciae symbiotic hydrogenase activity and processing are limited by the level of nickel in agricultural soils
Ni
Solidesulfovibrio fructosivorans
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contains FeNi-center
Ni
Solidesulfovibrio fructosivorans
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contains Ni in the catalytic center
Ni
Solidesulfovibrio fructosivorans
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contains Ni-Fe bimetallic center as active site
Ni
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contains 1 g of atom of Ni per mol of protein
Ni
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0.6-0.7 atoms per mol enzyme
Ni2+
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essential element for the assembly and maturation, addition of 0.1 mM Ni2+ to the growth medium significantly enhances the hydrogenase activity. Nickel-treatment affects the level of the protein, but not the mRNA
Ni2+
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is composed of a large subunit, harboring the [NiFe] active site
Ni2+
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Ni-Fe active site assembly, nickel is absent in samples of HoxV
Ni2+
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[NiFeSe]-hydrogenase
Ni2+
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contains a Ni2+-binding site
Ni2+
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accessory protein HypB is necessary for Ni(II) incorporation into the hydrogenase protein. HypB has two metal-binding sites, a high-affinity Ni(II) site that includes ligands from the N-terminal domain and a low-affinity metal site located within the C-terminal GTPase domain
Ni2+
Megalodesulfovibrio gigas
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the active site has a characteristic bis(micro-thiolato)NiFe unit, where the Ni atom and the Fe atom are bridged by an undetermined oxygen-bearing ligand. This ligand probably derives from the aqueous solvent and is therefore most likely to be H2O, OH- or O2-. A NiFe or NiRu complex are not able to activate H2 when coordinated with an CH3CN ligand, thus a highly labile ligand that is simultaneously able to act as a Lewis base for the heterolytic activation of H2 is crucial to the action of H2ase. The CH3CN-coordinated Ni(II)Fe(II) complex is unstable in the presence of water and decomposed to the Ni(II) complex and the Fe(II) complex via the Fe-S bond cleavage in water. In order to synthesise H2O-coordinated NiFe complexes in aqueous media, the Lewis acidity of the Fe centre must be increased to form strong Fe-S bonds. Thus, organometallic ligands with a back-donating character to form Fe-C bonds are required
Ni2+
Solidesulfovibrio fructosivorans
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Sulfide
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7.2 mol labile sulfide per enzyme
Sulfide
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14.4 atoms per molecule
Sulfide
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10 atoms labile sulfide per mol enzyme
Sulfide
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12 atoms acid labile sulfur atoms per mol enzyme
Sulfide
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9.1 mol per mol enzyme, iron-sulfur protein
Sulfide
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10.8 mol acid labile sulfur per mol of enzyme
Sulfide
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24 g acid labile sulfide per 185 g enzyme