Hydrogen dehydrogenase
From Wikipedia, the free encyclopedia
In enzymology, a hydrogen dehydrogenase (EC 1.12.1.2) is an enzyme that catalyzes the chemical reaction
- H2 + NAD+ H+ + NADH
Thus, the two substrates of this enzyme are H2 and NAD+, whereas its two products are H+ and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is hydrogen:NAD+ oxidoreductase. Other names in common use include H2:NAD+ oxidoreductase, NAD+-linked hydrogenase, bidirectional hydrogenase, and hydrogenase. This enzyme participates in glyoxylate and dicarboxylate metabolism and methane metabolism. It has 6 cofactors: FAD, Iron, FMN, Flavin, Nickel, and Iron-sulfur.
[edit] References
- IUBMB entry for 1.12.1.2
- BRENDA references for 1.12.1.2 (Recommended.)
- PubMed references for 1.12.1.2
- PubMed Central references for 1.12.1.2
- Google Scholar references for 1.12.1.2
- BONE DH, BERNSTEIN S, VISHNIAC W (1963). "Purification and some properties of different forms of hydrogen dehydrogenase". Biochim. Biophys. Acta. 67: 581–8. doi: . PMID 13968752.
- Schneider K, Schlegel HG (1976). "Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16". Biochim. Biophys. Acta. 452: 66–80. PMID 186126.
[edit] External links
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- The CAS registry number for this enzyme class is 9027-05-8.