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Methionine sulfoxide cytochrome c.

K M Ivanetich, J J Bradshaw, L S Kaminsky

    Biochemistry
    |March 9, 1976
    PubMed
    Summary

    Chemical modification of cytochrome c specifically oxidizes methionine residues to methionine sulfoxide. This modification alters spectral properties and significantly lowers the redox potential, impacting its function in electron transport.

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    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Spectroscopy

    Background:

    • Cytochrome c is a crucial protein in cellular respiration.
    • Understanding its structure-function relationship is vital for cellular energy production.

    Purpose of the Study:

    • To investigate the effects of specific chemical modification on cytochrome c.
    • To elucidate the role of methionine residues in cytochrome c's structure and function.

    Main Methods:

    • Methylene blue-mediated photooxidation to modify methionine residues.
    • Spectroscopic analysis (absorbance, circular dichroism) to assess structural changes.
    • Redox potential measurements to evaluate functional impact.

    Main Results:

    • Methionine residues were selectively oxidized to methionine sulfoxide without affecting other residues.
    • Spectral changes observed, including loss of 695 nm absorbance and altered Soret band.
    • Redox potential decreased from 260 mV to 184 mV.
    • Modified cytochrome c showed altered interaction with succinate-cytochrome c reductase but remained functional for cytochrome oxidase.

    Conclusions:

    • Methionine-80 plays a key role in maintaining a closed hydrophobic heme crevice.
    • This crevice is essential for preserving the native redox potential of cytochrome c.
    • The modification provides insights into the structural requirements for cytochrome c's electron transfer function.

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