The interactions between cytochrome c and cytochrome oxidase that determine the conformation of the oxidized oxidase
- 1 April 1977
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 55 (4) , 458-464
- https://doi.org/10.1139/o77-064
Abstract
Cytochrome c2+ increases the rate at which cytochrome oxidase (EC 1.9.3.1) .lambda.max 428 nm) converts to its conformation isomer (.lambda.max 418-423 nm) but cytochrome c3+ has little effect on the conversion rate. Interactions between reduced cytochrome oxidase and cytochrome c were studied in the absence of electron flow using anaerobic Sephadex columns. Oxidase that is reduced by cytochrome c2+ or other reductant forms the 418- to 423-nm isomer if its last contact, before oxidation, is with cytochrome c3+. If the reduced oxidase contacts cytochrome c2+ before oxidation, the 428-nm oxidase forms.This publication has 5 references indexed in Scilit:
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