[NiFe] hydrogenase is a type of hydrogenase, which is an oxidative enzyme that reversibly converts molecular hydrogen in prokaryotes including Bacteria and Archaea.[1][2] The catalytic site on the enzyme provides simple hydrogen-metabolizing microorganisms a redox mechanism by which to store and utilize energy via the reaction
This is particularly essential for the anaerobic, sulfate-reducing bacteria of the genus Desulfovibrio[3][4] as well as pathogenic organisms Escherichia coli and Helicobacter pylori.[2] The mechanisms, maturation, and function of [NiFe] hydrogenases are actively being researched for applications to the hydrogen economy and as potential antibiotic targets.
^Jugder, Bat-Erdene; Welch, Jeffrey; Aguey-Zinsou, Kondo-Francois; Marquis, Christopher P. (2013-05-14). "Fundamentals and electrochemical applications of [Ni–Fe]-uptake hydrogenases". RSC Advances. 3 (22): 8142. doi:10.1039/c3ra22668a. ISSN 2046-2069.
^ abVignais, Paulette M.; Billoud, Bernard (October 2007). "Occurrence, Classification, and Biological Function of Hydrogenases: An Overview". Chemical Reviews. 107 (10): 4206–4272. doi:10.1021/cr050196r. PMID 17927159.
^Volbeda, A.; Garcin, E.; Piras, C.; de Lacey, A. L.; Fernandez, V. M.; Hatchikian, E. C.; Frey, M.; Fontecilla-Camps, J. C. (1996). "Structure of the [NiFe] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands". J. Am. Chem. Soc. 118 (51): 12989–12996. doi:10.1021/ja962270g.
^Eidsness, M. K.; Scott, R. A.; Prickril, B. C.; DerVartanian, D. V.; Legall, J.; Moura, I.; Moura, J. J.; Peck, H. D. (1989). "Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus". Proceedings of the National Academy of Sciences. 86 (1): 147–151. doi:10.1073/pnas.86.1.147. PMC 286421. PMID 2521386.
[NiFe] hydrogenase is a type of hydrogenase, which is an oxidative enzyme that reversibly converts molecular hydrogen in prokaryotes including Bacteria...
nickel-iron hydrogenase, and iron hydrogenase. Hydrogenases catalyze, sometimes reversibly, H2 uptake. The [FeFe] and [NiFe] hydrogenases are true redox...
Fontecilla-Camps, J. (1996). "Structure of the [NiFe] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands". J. Am. Chem. Soc. 118 (51): 12989–12996...
networks. These hybrids have been prepared using [FeFe] and [NiFe] hydrogenases. The [NiFe] hydrogenase isolated from A. aeolicus (thermophilic bacteria)...
cyanide. The hydrogenase enzymes contain cyanide ligands attached to iron in their active sites. The biosynthesis of cyanide in the NiFehydrogenases proceeds...
compounds of the [Fe] hydrogenase. More recently Manor and Rauchfuss presented a very interesting mimic compound based in the [NiFe] hydrogenase with bidirectional...
hydrogenase maturation protease family is a family of aspartic endopeptidases belonging to MEROPS family A31. The large subunit of [NiFe]-hydrogenase...
[NiFe]-hydrogenases were obtained. In the course of this work a 0.89 Ångström resolution X-ray crystallography diffraction model of [NiFe]-hydrogenase...
oxidation state is important to nickel-containing enzymes, such as [NiFe]-hydrogenase, which catalyzes the reversible reduction of protons to H2. Nickel(II)...
hydrogenase, and iron hydrogenase. All hydrogenases catalyze reversible H2 uptake, but while the [FeFe] and [NiFe] hydrogenases are true redox catalysts...
ferredoxin hydrogenase (EC 1.12.7.2), also referred to as [Fe-Fe] hydrogenase, H2 oxidizing hydrogenase, H2 producing hydrogenase, bidirectional hydrogenase, hydrogenase...
Maurice van Gastel; Wolfgang Lubitz (2009). "EPR Investigation of [NiFe] Hydrogenases". In Graeme Hanson; Lawrence Berliner (eds.). High Resolution EPR:...
[FeFe]-hydrogenases have a Fe2(μ-SR)2(μ-CO)(CO)2(CN)2 active site connected to a 4Fe4S cluster via a bridging thiolate. The active site of the [NiFe]-hydrogenases...
blue copper proteins, iron in cytochrome P450, and nickel in the [NiFe]-hydrogenases. The sulfhydryl group also has a high affinity for heavy metals, so...
"Structure and Electron Transfer Pathways of an Electron-Bifurcating NiFe-Hydrogenase". Science Advances. 8 (8): eabm7546. doi:10.1126/sciadv.abm7546. PMC 8880783...
"Structural and Functional Analogues of the Active Sites of the [Fe]-, [NiFe]-, and [FeFe]-Hydrogenases". Chemical Reviews. 109 (6): 2245–2274. doi:10.1021/cr800542q...
active site metal content: [FeFe]-hydrogenases (iron-iron), [NiFe]-hydrogenases (nickel-iron) hydrogenases, and [Fe]-hydrogenases (iron-only). Many organisms...
"Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus". Proceedings...
endopeptidase HycI from Escherichia coli: implications for mechanism of the [NiFe] hydrogenase maturation". The Journal of Biological Chemistry. 282 (6): 3856–63...
{\displaystyle {\ce {H2}}} using two membrane-associated, oxygen-dependent [NiFe] hydrogenases". Proceedings of the National Academy of Sciences. 111 (11): 4257–4261...
[NiFe]-hydrogenase. The reaction being H 2 ⟷ 2 H + + 2 e − {\displaystyle H_{2}\longleftrightarrow 2H^{+}+2e^{-}} . There are many different [NiFe]-hydrogenases...
was present, which is required for thiosulfate oxidation. It lacks NiFehydrogenase (hyaB) and formate dehydrogenase genes (fdhA), indicating that it cannot...
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