Biology:Carbon-monoxide dehydrogenase (ferredoxin)
From HandWiki
carbon-monoxide dehydrogenase (ferredoxin) | |||||||||
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Identifiers | |||||||||
EC number | 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 | ||||||||
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In enzymology, a carbon-monoxide dehydrogenase (ferredoxin) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
- CO + H2O + oxidized ferredoxin [math]\displaystyle{ \rightleftharpoons }[/math] CO2 + reduced ferredoxin
The 3 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
- "Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans". Journal of Bacteriology 141 (1): 74–80. 1980. doi:10.1128/jb.141.1.74-80.1980. PMID 7354006.
- "Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein". Journal of Biological Chemistry 258 (4): 2364–9. 1983. doi:10.1016/S0021-9258(18)32932-6. PMID 6687389.
- "A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase". Science 298 (5593): 567–72. 2002. doi:10.1126/science.1075843. PMID 12386327. Bibcode: 2002Sci...298..567D.
![]() | Original source: https://en.wikipedia.org/wiki/Carbon-monoxide dehydrogenase (ferredoxin).
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