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Related Experiment Videos

Do evolutionary changes in cytochrome c structure reflect functional adaptations?

E Margoliash, S Ferguson-Miller, C H Kang

    Federation Proceedings
    |August 1, 1976
    PubMed
    Summary
    This summary is machine-generated.

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    Evolutionary changes in cytochrome c are not constant, challenging neutral mutation theory. A high-affinity reaction with cytochrome c oxidase reveals species-specific differences, suggesting a role in mitochondrial respiratory control.

    Area of Science:

    • Biochemistry
    • Evolutionary Biology
    • Molecular Biology

    Background:

    • The rate of evolutionary change in eukaryotic cytochromes c amino acid sequences is variable, questioning the dominance of neutral mutations.
    • Previous research indicated functional indistinguishability of eukaryotic cytochromes c in mitochondrial respiratory chain interactions.

    Purpose of the Study:

    • To investigate potential functional differences in cytochrome c from various species.
    • To explore the kinetics of cytochrome c interaction with cytochrome c oxidase.
    • To assess the role of nucleotides in modulating this interaction and its implications for mitochondrial respiratory control.

    Main Methods:

    • Kinetic analysis of cytochrome c reactions with cytochrome c oxidase at low ionic strength.
    • Direct binding studies to determine dissociation constants.

    Related Experiment Videos

  • Investigation of inhibition by ADP and ATP at physiological concentrations.
  • Main Results:

    • A high-affinity reaction between cytochrome c and cytochrome c oxidase was discovered, with significant activity differences among species (horse, yeast, Euglena).
    • Observed Km values (10^-7 to 10^-8 M) correlate with dissociation constants from binding studies.
    • The reaction is sensitive to ionic strength and inhibited by ADP and ATP, with ATP being more potent.

    Conclusions:

    • Functional differences in cytochrome c exist, contradicting previous assumptions of indistinguishability.
    • The ATP-mediated inhibition of cytochrome c binding to its oxidase suggests a novel mechanism for mitochondrial respiratory control.
    • These findings open avenues for studying evolutionary adaptations of cytochromes c in relation to their oxidases.