Hydrogen:quinone oxidoreductase
hydrogen:quinone oxidoreductase | |||||||||
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Identifiers | |||||||||
EC no. | 1.12.5.1 | ||||||||
CAS no. | 147097-29-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a hydrogen:quinone oxidoreductase (EC 1.12.5.1) is an enzyme that catalyzes the chemical reaction
- H2 + quinone quinol
Thus, the two substrates of this enzyme are H2 and quinone, whereas its product is quinol. The quinone can be menaquinone, ubiquinone, or .
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.
Categories:
- EC 1.12.5
- Enzymes of unknown structure
- Oxidoreductase stubs