Hydrogenase (NAD+, ferredoxin)
| Hydrogenase (NAD+, ferredoxin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.12.1.4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Hydrogenase (NAD+, ferredoxin) (EC 1.12.1.4, bifurcating [FeFe] hydrogenase) is an enzyme with systematic name hydrogen:NAD+, ferredoxin oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
- 2 H2 + NAD+ + 2 oxidized ferredoxin 5 H+ + NADH + 2 reduced ferredoxin
The enzyme from Thermotoga maritima contains a [Fe-Fe] cluster (H-cluster) and iron-sulfur clusters. I
References
- ↑ Verhagen, M.F.; O'Rourke, T.; Adams, M.W. (1999). "The hyperthermophilic bacterium, Thermotoga maritima, contains an unusually complex iron-hydrogenase: amino acid sequence analyses versus biochemical characterization". Biochim. Biophys. Acta. 1412 (3): 212–229. doi:10.1016/s0005-2728(99)00062-6. PMID 10482784.
- ↑ Schut, G.J.; Adams, M.W. (2009). "The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production". J. Bacteriol. 191 (13): 4451–4457. doi:10.1128/JB.01582-08. PMC 2698477
. PMID 19411328.
External links
- Hydrogenase (NAD , ferredoxin) at the US National Library of Medicine Medical Subject Headings (MeSH)
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