Spectral Properties of Cytochrome b-561 and Cytochrome b-565 in Mucidin-Resistant Mutants of Saccharomyces cerevisiae

Abstract
The oxidation of NADH in submitochondrial particles isolated from MUC1, MUC2 and MUC3 mucidin-resistant mutants of S. cerevisiae is specifically resistant to mucidin. Extra reduction of cytochrome b-565 induced by mucidin is demonstrated in all tested mucidin-resistant mutants. Red shift of cytochrome b-561 is induced by mucidin in 2 independent MUC3 mutants. In MUC1 and MUC2 mutants, the red shift is not induced by mucidin, while that promoted by antimycin A and 2-n-heptyl-4-hydroxyquinoline N-oxide are normal. Apparently, the extra reduction of cytochrome b-565 and the red shift of cytochrome b-561 elicited by mucidin can be largely dissociated from the overall inhibition of the electron flow by distinct mucidin-resistant mutations in different exons of the split mitochondrial gene of cytochrome b.

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