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Related Experiment Videos

Subunit structure of electron transfer flavoprotein.

M C McKean, J D Beckmann, F E Frerman

    The Journal of Biological Chemistry
    |February 10, 1983
    PubMed
    Summary

    Pig liver mitochondrial electron transfer flavoprotein has nonidentical subunits (31,000 and 27,000 daltons), clarifying its structure and FAD content. This protein links dehydrogenases to the electron transport system.

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    Area of Science:

    • Biochemistry
    • Mitochondrial respiration
    • Protein structure

    Background:

    • Electron transfer flavoprotein (ETF) from pig liver mitochondria is a key electron transferase.
    • It links primary flavoprotein dehydrogenases to the mitochondrial electron transport system.
    • Previous literature reported conflicting FAD content and suggested identical subunits.

    Purpose of the Study:

    • To resolve conflicting reports on ETF subunit composition and FAD content.
    • To elucidate the precise molecular structure of pig liver ETF.
    • To investigate the heterogeneity of ETF subunits.

    Main Methods:

    • Polyacrylamide gel electrophoresis in 8 M urea and SDS.
    • Cyanogen bromide peptide mapping of subunits.
    • Amino acid analysis of protein and subunits.
    • Spectrophotometric determination of FAD content.

    Main Results:

    • ETF consists of nonidentical subunits with molecular weights of 31,000 and 27,000 daltons.
    • Peptide analysis confirmed different primary structures for the subunits.
    • Amino acid analyses ruled out proteolysis as the cause of heterogeneity.
    • The protein contains 1 mol of FAD per mole of protein.

    Conclusions:

    • Pig liver ETF is a heterodimer with distinct subunits.
    • The observed heterogeneity is inherent to the protein structure, not due to degradation.
    • This clarifies the molecular basis of ETF function in electron transfer pathways.

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