Reactions of cytochrome c oxidase with sodium dithionite
- 1 January 1983
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 209 (1), 175-182
- https://doi.org/10.1042/bj2090175
Abstract
The reduction of [bovine heart] cytochrome c oxidase by dithionite was investigated by stopped-flow spectrophotometry and flow-flash techniques in the presence of CO. Of the 2 heme groups present in the enzyme, that associated with cytochrome a is the first reduced. The second-order rate constants for reduction of a number of redox proteins (cytochrome c, [Rhus vernicifera] stellacyanin and [Pseudomonas aeruginosa] azurin) by the S2O42- 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.This publication has 20 references indexed in Scilit:
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