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Studies on electron transfer between mercury electrode and hemoprotein

F Scheller, M Jänchen, J Lampe

    Biochimica Et Biophysica Acta
    |November 18, 1975
    PubMed
    Summary
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    Electrochemical studies reveal hemoproteins undergo structural changes upon adsorption, with charge transfer occurring via adsorbed molecules. The protein

    Area of Science:

    • Electrochemistry
    • Biochemistry
    • Protein science

    Background:

    • Hemoproteins like ferricytochrome c, metmyoglobin, and methemoglobin are crucial in biological systems.
    • Understanding their electrochemical properties is key to elucidating electron transfer mechanisms.

    Purpose of the Study:

    • To investigate the electrochemical behavior of ferricytochrome c, metmyoglobin, and methemoglobin.
    • To determine the influence of adsorption on charge transfer processes.
    • To assess the impact of electrochemical reactions on protein structure and function.

    Main Methods:

    • Direct current (d.c.) polarography
    • Alternating current (a.c.) polarography
    • Differential pulse polarography
    • Controlled potential electrolysis

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    Main Results:

    • All three hemoproteins exhibited concentration-dependent polarographic steps and peaks, indicating charge transfer influenced by strong adsorption.
    • Alternating current polarography revealed structural modifications in adsorbed hemoprotein molecules.
    • Electrolyzed metmyoglobin and methemoglobin retained native spectral properties, with unaffected oxygen affinity and hemoglobin cooperativity.

    Conclusions:

    • Electrochemical reactions at the electrode surface do not compromise the fundamental functions of metmyoglobin and methemoglobin.
    • Charge transfer involves adsorbed, reduced protein intermediates before transfer to freely diffusible proteins.
    • The study provides insights into the electrochemical interface behavior of key hemoproteins.