Thus, the two substrates of this enzyme are H₂ and quinone, whereas its product is quinol. The quinone can be menaquinone, ubiquinone, demethylmenaquinone or methionaquinone.

This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with a quinone or similar compound as acceptor. The systematic name of this enzyme class is hydrogen:quinone oxidoreductase. Other names in common use include hydrogen-ubiquinone oxidoreductase, hydrogen:menaquinone oxidoreductase, membrane-bound hydrogenase, and quinone-reactive Ni/Fe-hydrogenase.

References

E, Duchene A, Tripier D, Juvenal K, et al. (1992). "The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes". Eur. J. Biochem. 206 (1): 93–102. doi:10.1111/j.1432-1033.1992.tb16905.x. PMID 1587288.
E, Duchene A, Tripier D, Juvenal K, et al. (1993). "The quinone-reactive Ni/Fe-hydrogenase of Wolinella Succinogenes". Eur. J. Biochem. 214 (3): 949–50. doi:10.1111/j.1432-1033.1993.tb17999.x. PMID 8319698.
Gross R, Simon J, Lancaster CR, Kröger A (1998). "Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2". Mol. Microbiol. 30 (3): 639–46. doi:10.1046/j.1365-2958.1998.01100.x. PMID 9822828.
Bernhard M, Benelli B, Hochkoeppler A, Zannoni D, Friedrich B (1997). "Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16". Eur. J. Biochem. 248 (1): 179–86. doi:10.1111/j.1432-1033.1997.00179.x. PMID 9310376.
Ferber DM, Maier RJ (1993). "Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium japonicum membrane-bound hydrogenase". FEMS Microbiol. Lett. 110 (3): 257–64. doi:10.1111/j.1574-6968.1993.tb06331.x. PMID 8354459.
Kodama T (1991). "Methionaquinone is a direct natural electron-acceptor for the membrane-bound hydrogenase in Hydrogenobacter thermophilus strain TK-6". Agric. Biol. Chem. 55: 3011–3016. doi:10.1271/bbb1961.55.3011.
Infossi, Pascale; Lojou, Elisabeth; Chauvin, Jean-Paul; Herbette, Gaetan; Brugna, Myriam; Giudici-Orticoni, Marie-Thérèse (2010). "Aquifex aeolicus membrane hydrogenase for hydrogen biooxidation: Role of lipids and physiological partners in enzyme stability and activity". International Journal of Hydrogen Energy. 35 (19): 10778–10789. doi:10.1016/j.ijhydene.2010.02.054. ISSN 0360-3199.
Frielingsdorf, Stefan; Schubert, Torsten; Pohlmann, Anne; Lenz, Oliver; Friedrich, Bärbel (2011). "A Trimeric Supercomplex of the Oxygen-Tolerant Membrane-Bound [NiFe]-Hydrogenase fromRalstonia eutrophaH16". Biochemistry. 50 (50): 10836–10843. doi:10.1021/bi201594m. ISSN 0006-2960.
Radu, Valentin; Frielingsdorf, Stefan; Evans, Stephen D.; Lenz, Oliver; Jeuken, Lars J. C. (2014). "Enhanced Oxygen-Tolerance of the Full Heterotrimeric Membrane-Bound [NiFe]-Hydrogenase ofRalstonia eutropha". Journal of the American Chemical Society. 136 (24): 8512–8515. doi:10.1021/ja503138p. ISSN 0002-7863. PMC 4073834. PMID 24866391.

v t e Oxidoreductases: Acting on hydrogen as donor (EC 1.12)
1.12.1	Hydrogen dehydrogenase Hydrogen dehydrogenase (NADP+) Hydrogenase (NAD+, ferredoxin)
1.12.2	Cytochrome-c3 hydrogenase
1.12.5	Hydrogen:quinone oxidoreductase
1.12.7	Ferredoxin hydrogenase
1.10.98	Coenzyme F420 hydrogenase 5,10-Methenyltetrahydromethanopterin hydrogenase Methanosarcina-phenazine hydrogenase Sulfhydrogenase
1.10.99	Hydrogenase (acceptor)

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)