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Related Experiment Videos

Redox conformation changes in refined tuna cytochrome c.

T Takano, R E Dickerson

    Proceedings of the National Academy of Sciences of the United States of America
    |November 1, 1980
    PubMed
    Summary

    High-resolution X-ray crystallography reveals subtle conformational changes in tuna ferrocytochrome c and ferricytochrome c. These shifts impact the heme microenvironment and active site structure, offering insights into electron transfer mechanisms.

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    Area of Science:

    • Biochemistry
    • Structural Biology
    • Crystallography

    Background:

    • Cytochrome c is a crucial protein in cellular respiration.
    • Understanding its structure is key to elucidating electron transfer processes.

    Purpose of the Study:

    • To determine the high-resolution crystal structures of tuna ferrocytochrome c and ferricytochrome c.
    • To identify structural differences between the oxidized and reduced states.

    Main Methods:

    • X-ray crystallography at 1.5 A and 1.8 A resolution.
    • Refinement of ferrocytochrome c and ferricytochrome c structures.
    • Analysis of conformational differences and heme microenvironment.

    Main Results:

    • Identified significant conformational differences around a buried water molecule.

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  • Observed changes in water molecule proximity to the heme and heme position in the oxidized state.
  • These changes create a more polar microenvironment for the heme.

    • Conclusions:

    • The active site of cytochrome c is defined by specific lysine residues and the 72-87 loop.
    • A buried water molecule and heme crevice opening influence the heme's microenvironment.
    • Structural variations correlate with function and evolutionary conservation.