| Literature DB >> 6303299 |
G D Jones, M G Jones, M T Wilson, M Brunori, A Colosimo, P Sarti.
Abstract
The reduction of cytochrome c oxidase (EC 1.9.3.1) by dithionite was investigated by stopped-flow spectrophotometry and flow-flash techniques in the presence of CO. Of the two haem groups present in the enzyme, that associated with cytochrome alpha is the first reduced. The second-order rate constants for reduction of a number of redox proteins (cytochrome c, stellacyanin and azurin) by the S2O4(2-) and SO2.- anions are reported, and the values are compared with those determined for cytochrome c oxidase. These results are discussed in terms of the accessibility and charge distribution of the electron-entry site of cytochrome c oxidase.Entities:
Mesh:
Substances:
Year: 1983 PMID: 6303299 PMCID: PMC1154069 DOI: 10.1042/bj2090175
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857