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. 1976 May 1;155(2):453–455. doi: 10.1042/bj1550453

Kinetic studies on the binding of cyanide to oxygenated cytochrome c oxidase.

T Brittain, C Greenwood
PMCID: PMC1172854  PMID: 180986

Abstract

The reaction of cyanide with oxygenated cytochrome c oxidase was followed by means of flow-flash techniques. The oxygenated form, produced after photolysis of the partially reduced CO complex in the presence of cyanide and O2, shows cyanide-binding properties distinct from those of both the oxidized and the reduced forms of the protein. The binding is a single process (k = 22M-1-S-1) linearly dependent on cyanide concentration to as high as 75 mM. It is suggested that the oxygenated form is a conformational variant of the oxidized protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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