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A hydrogenase is an enzyme that catalyses the reversible oxidation of molecular hydrogen (H2). Hydrogenases play a vital role in anaerobic metabolism. Hydrogen uptake (H2 oxidation) (1) is coupled to the reduction of electron acceptors such as oxygen, nitrate, sulfate, carbon dioxide, and fumarate, whereas proton reduction (H2 evolution) (2) is essential in pyruvate fermentation and in the disposal of excess electrons. Both low-molecular weight compounds and proteins such as ferredoxins, cytochrome c3, and cytochrome c6 can act as physiological electron donors (D) or acceptors (A) for hydrogenases: H2 + Aox → 2H+ + Ared (1) 2H+ + Dred → H2 + Dox (2) Hydrogenases were first discovered in the 1930s, and they have attracted interest from many researchers. The mechanism of the catalysis of hydrogenase might help scientists design clean biological energy sources, such as algae, that produce hydrogen molecules.*.
Biochemical classification EC 1.12.1.2 hydrogen dehydrogenase (hydrogen:NAD+ oxidoreductase) H2 + NAD+ = H+ + NADH EC 1.12.1.3 hydrogen dehydrogenase (NADP) (hydrogen:NADPH+ oxidoreductase) H2 + NADP+ = H+ + NADPH EC 1.12.2.1 cytochrome-c3 hydrogenase (hydrogen:ferricytochrome-c3 oxidoreductase) 2H2 + ferricytochrome c3 = 4H+ + ferrocytochrome c3 EC 1.12.7.2 ferredoxin hydrogenase (hydrogen:ferredoxin oxidoreductase) H2 + oxidized ferredoxin = 2H+ + reduced ferredoxin EC 1.12.98.1 coenzyme F420 hydrogenase (hydrogen:coenzyme F420 oxidoreductase) H2 + coenzyme F420 = reduced coenzyme F420 EC 1.12.99.6 hydrogenase (acceptor) (hydrogen:acceptor oxidoreductase) H2 + A = AH2 EC 1.12.5.1 hydrogen:quinone oxidoreductase H2 + menaquinone = menaquinol EC 1.12.98.2 5,10-methenyltetrahydromethanopterin hydrogenase (hydrogen:5,10-methenyltetrahydromethanopterin oxidoreductase) H2 + 5,10-methenyltetrahydromethanopterin = H+ + 5,10-methylenetetrahydromethanopterin EC 1.12.98.3 Methanosarcina-phenazine hydrogenase hydrogen:2-(2,3-dihydropentaprenyloxy)phenazine oxidoreductase H2 + 2-(2,3-dihydropentaprenyloxy)phenazine = 2-dihydropentaprenyloxyphenazine Structural classification Until 2004, hydrogenases were classified according to the metals thought to be at their active sites; three classes were recognized: iron-only (Fe-only), nickel-iron (NiFe), and "metal-free". In 2004, Thauer et al. showed that the metal-free hydrogenases in fact contain iron. Thus those enzymes previously called "metal-free" are now named "FeS-free", since this protein contains no inorganic sulfide in contrast to the Fe-only enzymes. In some Ni-Fe hydrogenases, one of the Ni-bound cysteine residues is replaced by selenocysteine. On the basis of sequence similarity, however, the Ni-Fe and Ni-Fe-Se hydrogenases should be considered a single superfamily. The Ni-Fe hydrogenases are heterodimeric proteins consisting of small (S) and large (L) subunits. The small subunit contains three iron-sulfur clusters while the large subunit contains a nickel-iron centre. Periplasmic, cytoplasmic, and cytoplasmic membrane-bound hydrogenases have been found. The Ni-Fe hydrogenases, when isolated, are found to catalyse both H2 evolution and uptake, with low-potential multihaem cytochromes such as cytochrome c3 acting as either electron donors or acceptors, depending on their oxidation state. The hydrogenases containing no other metal than iron are called Fe hydrogenases (Fe-Hases) or Fe-only hydrogenases. Three families of Fe-Hases are recognized: (I) cytoplasmic, soluble, monomeric Fe-Hases, found in strict anaerobes such as Clostridium pasteurianum and Megasphaera elsdenii. They are extremely sensitive to inactivation by dioxygen (O2) and catalyse both H2 evolution and uptake. (II) periplasmic, heterodimeric Fe-Hases from Desulfovibrio spp., which can be purified aerobically and catalyse mainly H2 oxidation. (III) soluble, monomeric Fe-Hases, found in chloroplasts of green alga Scenedesmus obliquus, catalyses H2 evolution. The Fe2S2 ferredoxin functions as natural electron donor linking the enzyme to the photosynthetic electron transport chain. Ni-Fe and Fe-only hydrogenases have some common features in their structures: each enzyme has an active site and a few Fe-S clusters that are buried in protein. The active site, which is believed to be the place where catalysis takes place, is also a metallocluster, and each metal is coordinated by carbon monoxide (CO) and cyanide (CN-) ligands. 5,10-methenyltetrahydromethanopterin hydrogenase (EC 1.12.98.2) found in methanogenic Achaea contains neither nickel nor iron-sulfur clusters but an iron-containing cofactor of yet unknown structure, presumably a pyridone GMP derivative | ||||||||
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