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Models for metal-sulfur coordination in copper proteins.

M Younes, W Pilz, U Weser

    Journal of Inorganic Biochemistry
    |February 1, 1979
    PubMed
    Summary

    X-ray photoelectron spectrometry revealed copper(I) in model compounds with copper-sulfur bonds. These compounds, similar to blue copper proteins, react with superoxide radicals, suggesting electron delocalization in the metal-sulfur chromophore.

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    Area of Science:

    • Biochemistry
    • Inorganic Chemistry
    • Spectroscopy

    Background:

    • Copper-sulfur chromophores are essential in biological systems, particularly in blue copper proteins.
    • Understanding the oxidation state and electronic properties of copper in these environments is crucial for elucidating their function.
    • Model compounds are vital for studying the complex interactions within metalloproteins.

    Purpose of the Study:

    • To determine the oxidation state of copper in model compounds containing copper-sulfur bonds.
    • To investigate the reactivity of these model compounds with superoxide anion radicals.
    • To propose a model for electron delocalization in the metal-sulfur chromophore of blue copper proteins.

    Main Methods:

    • X-ray photoelectron spectrometry (XPS) was employed to analyze the oxidation state of copper.
    • Model compounds with copper coordinated to sulfur were synthesized and characterized.
    • Reactivity assays with superoxide anion radicals were performed.

    Main Results:

    • XPS analysis confirmed the presence of Cu(I) (3d10 state) in most studied copper-sulfur model compounds.
    • Photoreduction of copper was excluded as a factor in the observed oxidation states.
    • A model compound containing a Cu-S bond, Cu(ethylenediamine)2(SCN)2, was found to contain Cu(II) (3d9).
    • The model compounds exhibited significant reactivity towards superoxide anion radicals, mirroring the behavior of native parsley plastocyanin.

    Conclusions:

    • The study establishes Cu(I) as the predominant oxidation state in the investigated copper-sulfur model compounds.
    • The reactivity with superoxide suggests a delocalized electron system within the metal-sulfur chromophore.
    • A proposed equilibrium between RS--Cu(II) and RS.Cu(I) may explain the electronic properties of blue copper proteins.

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