PMID: 181272Aug 1, 1976

Do evolutionary changes in cytochrome c structure reflect functional adaptations?

Federation Proceedings
E MargoliashD L Brautigan

Abstract

Following the demonstration that the rate of evolutionary change in the amino acid sequences of cytochromes c of eukaryotic species was not constant either for a single line of phylogenetic descent during different evolutionary intervals or for separate lines of descent, the concept that neutral mutations account for the vast majority of the evolutionary variations could no longer be accepted. Previous studies had shown that all eukaryotic cytochromes c tested appeared to be functionally indistinguishable in their reaction with mitochondrial respiratory chain components. However, an examination of the kinetics at low ionic strength led to the discovery of a high affinity reaction of cytochrome c with cytochrome c oxidase that revealed large differences in activity between the cytochromes of the horse, baker's yeast and the protist Euglena. Observed Km values for this reaction of 10(-7) to 10(-8) M appear to represent actual dissociation constants, as demonstrated by direct binding studies of cytochrome c with purified cytochrome c oxidase. The high affinity reaction is sensitive to ionic strength and inhibited by ADP and ATP in the range of physiological concentrations, ATP being three times as effective as ADP. The possibility...Continue Reading

Related Concepts

Cytochrome C Oxidase
Cytochrome c Oxidase Subunit VIa
Acclimatization
Oxidase
Cytochrome c Group
Cytochromes
Mitochondria
Adaptation
Protein Conformation
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