Abstract
The 102-S-(2-thiopyridyl) and 102-S-(4-azidophenacyl) derivatives of yeast iso-1-cytochrome c have been prepared, both containing one mole of label per mole of cytochrome c. When the 102-S-(2-thiopyridyl) cytochrome c is allowed to interact with purified, detergent-solubilized yeast cytochrome oxidase, covalent crosslinked products are formed containing 0.9 to 0.98 moles of cytochrome c per oxidase. When the 102-S-(4-azidophenacyl) cytochrome c is exposed to the oxidase in the presence of ultraviolet light, covalently crosslinked products containing 0.2 to 0.35 moles of cytochrome c per oxidase are formed. SDS-polyacrylamide gel electrophoresis of these crosslinked products reveals the formation of a new band of apparent molecular weight 38,000 Daltons and the concurrent disappearance of subunit III (a crosslink of subunit III and cytochrome c). These affinity and photoaffinity crosslinking results are interpreted as evidence that the “backside” of yeast iso-1-cytochrome c interacts with subunit III of yeast cytochrome oxidase.
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