Hydrogen dehydrogenase

In enzymology, a hydrogen dehydrogenase (EC 1.12.1.2) is an enzyme that catalyzes the chemical reaction

H₂ + NAD⁺ ${\displaystyle \rightleftharpoons }$ 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 . It has 6 cofactors: FAD, Iron, FMN, Flavin, Nickel, and Iron-sulfur.

References[]

• BONE DH, BERNSTEIN S, VISHNIAC W (1963). "Purification and some properties of different forms of hydrogen dehydrogenase". Biochim. Biophys. Acta. 67: 581–8. doi:10.1016/0006-3002(63)91868-7. PMID 13968752.
• Schneider K, Schlegel HG (1976). "Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16". Biochim. Biophys. Acta. 452 (1): 66–80. doi:10.1016/0005-2744(76)90058-9. PMID 186126.