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词条 Carbon-monoxide dehydrogenase (cytochrome b-561)
释义

  1. References

{{enzyme
| Name = carbon-monoxide oxygenase
| EC_number = 1.2.2.4
| CAS_number = 64972-88-9
| IUBMB_EC_number = 1/2/2/4
| GO_code = 0008805
| image =
| width =
| caption =
}}

In enzymology, a carbon-monoxide dehydrogenase (cytochrome b-561) ({{EC number|1.2.2.4}}) is an enzyme that catalyzes the chemical reaction

CO + H2O + 2 ferricytochrome b-561 CO2 + 2 H+ + 2 ferrocytochrome b-561

The 3 substrates of this enzyme are CO, H2O, and ferricytochrome b-561, whereas its 3 products are CO2, H+, and ferrocytochrome b-561.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is carbon monoxide,water:cytochrome b-561 oxidoreductase. Other names in common use include carbon monoxide oxidase, carbon monoxide oxygenase (cytochrome b-561), carbon monoxide:methylene blue oxidoreductase, CO dehydrogenase, and carbon-monoxide dehydrogenase.

References

  • {{cite journal | vauthors = Meyer O, Jacobitz S, Kruger B | last-author-amp = yes | year = 1986 | title = Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria | journal = FEMS Microbiol. Rev. | volume = 39 | pages = 161–179 | doi=10.1111/j.1574-6968.1986.tb01858.x}}
  • {{cite journal | vauthors = Jacobitz S, Meyer O | year = 1989 | title = Removal of CO dehydrogenase from Pseudomonas carboxydovorans cytoplasmic membranes, rebinding of CO dehydrogenase to depleted membranes, and restoration of respiratory activities | journal = J. Bacteriol. | volume = 171 | pages = 6294–9 | pmid = 2808305 | issue=11 | pmc=210502}}
  • {{cite journal | vauthors = Meyer O, Schlegel HG | year = 1980 | title = Carbon monoxide:methylene blue oxidoreductase from Pseudomonas carboxydovorans | journal = J. Bacteriol. | volume = 141 | pages = 74–80 | pmid = 7354006 | issue=1 | pmc=293533}}
  • {{cite journal | vauthors = Dobbek H, Gremer L, Meyer O, Huber R | year = 1999 | title = Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | pages = 8884–9 | pmid = 10430865 | doi = 10.1073/pnas.96.16.8884 | pmc=17702}}
  • {{cite journal | vauthors = Hanzelmann P, Dobbek H, Gremer L, Huber R, Meyer O | year = 2000 | title = The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase | journal = J. Mol. Biol. | volume = 301 | pages = 1221–35 | pmid = 10966817 | doi = 10.1006/jmbi.2000.4023 }}
{{Aldehyde/Oxo oxidoreductases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{1.2-enzyme-stub}}

3 : EC 1.2.2|Enzymes of unknown structure|Carbon monoxide

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