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Carbon-monoxide dehydrogenase (ferredoxin)

From Wikipedia, the free encyclopedia

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.

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Transcription

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.


This page was last edited on 8 April 2024, at 07:48
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