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• W31766411 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." @default.
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• W31766411 date "1983-01-01" @default.
• W31766411 modified "2023-09-26" @default.
• W31766411 title "Reactions of cytochrome <i>c</i> oxidase with sodium dithionite" @default.
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• W31766411 doi "https://doi.org/10.1042/bj2090175" @default.
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