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Semisynthetic cytochrome c.

L E Barstow, R S Young, E Yakali

    Proceedings of the National Academy of Sciences of the United States of America
    |October 1, 1977
    PubMed
    Summary
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    Researchers created a functional horse heart cytochrome c using a synthetic peptide. This semisynthetic protein is identical to the naturally reconstituted version, demonstrating successful peptide synthesis and protein reassembly.

    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Molecular Biology

    Background:

    • Horse heart cytochrome c is crucial for cellular respiration.
    • Cytochrome c can be cleaved into heme and nonheme peptides.
    • Reconstitution of these peptides yields active cytochrome c.

    Purpose of the Study:

    • To synthesize a functional peptide fragment of horse heart cytochrome c using solid-phase synthesis.
    • To couple the synthesized nonheme peptide (residues 66-104) with the heme peptide (residues 1-65).
    • To evaluate the activity and properties of the resulting semisynthetic cytochrome c.

    Main Methods:

    • Chemical cleavage of horse heart cytochrome c using cyanogen bromide.
    • Merrifield solid-phase peptide synthesis for the nonheme fragment (residues 66-104).

    Related Experiment Videos

  • Complex formation and peptide linkage restoration to reassemble cytochrome c.

    • Main Results:

    • Successful synthesis of the nonheme peptide (residues 66-104).
    • Coupling of the heme peptide with the synthetic nonheme peptide.
    • The semisynthetic cytochrome c exhibited indistinguishable properties from reconstituted native cytochrome c.

    Conclusions:

    • Solid-phase peptide synthesis is a viable method for creating functional cytochrome c fragments.
    • Semisynthetic cytochrome c can be produced with full biological activity.
    • This approach offers a new avenue for studying and modifying cytochrome c structure-function relationships.