Carbon-monoxide dehydrogenase (ferredoxin)
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| carbon-monoxide dehydrogenase (ferredoxin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.7.4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a carbon-monoxide dehydrogenase (ferredoxin) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
- CO + H2O + oxidized ferredoxin CO2 + reduced ferredoxin
The three substrates of this enzyme are CO, H2O, and oxidized ferredoxin, whereas its two products are CO2 and reduced ferredoxin.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is carbon-monoxide,water:ferredoxin oxidoreductase.
References
- Meyer O, Schlegel HG (1980). "Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans". Journal of Bacteriology. 141 (1): 74–80. doi:10.1128/jb.141.1.74-80.1980. PMC 293533. PMID 7354006.
- Ragsdale SW, Clark JE, Ljungdahl LG, Lundie LL, Drake HL (1983). "Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein". Journal of Biological Chemistry. 258 (4): 2364–9. doi:10.1016/S0021-9258(18)32932-6. PMID 6687389.
- Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL (2002). "A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase". Science. 298 (5593): 567–72. Bibcode:2002Sci...298..567D. doi:10.1126/science.1075843. PMID 12386327.
