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. 1983 Jan 1;209(1):175–182. doi: 10.1042/bj2090175

Reactions of cytochrome c oxidase with sodium dithionite.

G D Jones, M G Jones, M T Wilson, M Brunori, A Colosimo, P Sarti
PMCID: PMC1154069  PMID: 6303299

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.

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Selected References

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