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.