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Complex formation between flavodoxin and cytochrome c. Cross-linking studies.

J L Dickerson, J J Kornuc, D C Rees

    The Journal of Biological Chemistry
    |April 25, 1985
    PubMed
    Summary

    Cross-linking studies demonstrate complex formation between Azotobacter vinelandii flavodoxin and horse cytochrome c. The determined association constant supports a structural model compatible with kinetic data for electron transfer.

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    Area of Science:

    • Biochemistry
    • Protein-protein interactions
    • Electron transfer mechanisms

    Background:

    • Azotobacter vinelandii flavodoxin and horse cytochrome c are key proteins in electron transfer pathways.
    • Understanding their interaction is crucial for elucidating biological redox processes.

    Purpose of the Study:

    • To demonstrate and characterize the complex formation between Azotobacter vinelandii flavodoxin and horse cytochrome c.
    • To compare the structural and binding properties of the cross-linked complex with kinetically identified complexes.

    Main Methods:

    • Utilized chemical cross-linking agents including dimethyl suberimidate, dimethyl adipimidate, 1-ethyl-3-(3-di-methylaminopropyl)carbodiimide, and dimethyl-3,3'-dithiobispropionimidate.
    • Quantified protein complexation at varying ionic strengths.

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  • Determined the association constant of the protein complex.

    • Main Results:

    • Established complex formation between Azotobacter vinelandii flavodoxin and horse cytochrome c using multiple cross-linking reagents.
    • Observed quantitative cross-linking with carbodiimide reagents at low ionic strengths.
    • Calculated an association constant of 4 x 10(4) M-1 at 88 mM ionic strength.

    Conclusions:

    • The cross-linked complex exhibits binding characteristics similar to the kinetically determined precursor complex.
    • The findings support a proposed structural model for the flavodoxin-cytochrome c complex.
    • Cross-linking provides a valuable method for studying transient protein-protein interactions in electron transfer systems.