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A model for cytochrome oxidase.

G Palmer, G T Babcock, L E Vickery

    Proceedings of the National Academy of Sciences of the United States of America
    |July 1, 1976
    PubMed
    Summary
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    A new model for cytochrome c oxidase proposes distinct spin states for its cytochromes a and a3. Enzyme conformational changes upon reduction expose coordination sites, explaining spectroscopic and magnetic data.

    Area of Science:

    • Biochemistry
    • Biophysics
    • Enzymology

    Background:

    • Cytochrome c oxidase is a crucial metalloenzyme in cellular respiration.
    • Understanding its active site structure and function is key to deciphering electron transfer mechanisms.

    Purpose of the Study:

    • To propose a novel structural model for the active center of cytochrome c oxidase.
    • To explain diverse experimental observations using this proposed model.

    Main Methods:

    • Theoretical modeling of the enzyme's active center.
    • Analysis of data from magnetic circular dichroism (MCD) spectroscopy.
    • Interpretation of Mossbauer spectroscopy results.
    • Evaluation of electron paramagnetic resonance (EPR) spectroscopy data.
    • Consideration of magnetic susceptibility measurements.

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    Main Results:

    • The model posits cytochrome a as a low-spin ferrihemoprotein.
    • Cytochrome a3 is proposed as a high-spin ferrihemoprotein antiferromagnetically coupled to a Cu2+ ion.
    • Enzyme reduction induces a conformational change, exposing a coordination site on cytochrome a3.

    Conclusions:

    • The proposed model successfully accounts for various spectroscopic and magnetic properties of cytochrome c oxidase.
    • This model provides a framework for understanding the enzyme's mechanism of action.