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Electronic and Geometric Structure of the CuA Site Studied by 1H NMR in a Soluble Domain of Cytochrome c Oxidase from Paracoccus denitrificans

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    Electronic and Geometric Structure of the CuA Site Studied by 1H NMR in a Soluble Domain of Cytochrome c Oxidase from Paracoccus denitrificans
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    Contribution from the Department of Chemistry, University of Florence, Via Gino Capponi 7, 50121 Florence, Italy, Department of Soil Science and Plant Nutrition, University of Florence, P.le delle Cascine 28, 50144 Florence, Italy, European Molecular Biology Laboratory, 69012 Heidelberg, Germany, and Department of Biochemistry and Biophysics, Göteborg University, Göteborg, Sweden
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 1997, 119, 45, 11023–11027
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    https://doi.org/10.1021/ja9715399
    Published November 12, 1997
    Copyright © 1997 American Chemical Society
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    Abstract

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    An extensive assignment of the 1H NMR spectra of a CuA domain from the cytochrome c oxidase of Paracoccus denitrificans has been obtained on the basis of dipolar connectivities coupled to the available structural information. The assignment has been extended with the aid of 2H NMR spectra on a protein sample with cysteines selectively labeled at the β position. The spectra have been compared to those published earlier for a similar CuA fragment from the Thermus thermophilus oxidase and for a CuA construct in a blue copper protein, amicyanin. The shifts and their temperature dependence are discussed in terms of molecular orbital descriptions available for these systems. The mechanisms for the fast electron relaxation, which make the obtainment of relatively sharp NMR signals possible, are discussed. It is shown that the proton shifts of one histidine are variable from one system to the other, possibly reflecting changes in its interaction with the Cu2S2 diamond structure. Large electron delocalization onto the S atoms is confirmed. This is reflected in the large shifts experienced by the cysteine β-CH2 protons, and these shifts are in turn tuned by the Cu−S−C−H torsion angles. It is suggested that the electronic structure of CuA is ideal for its function in electron transfer.

    Copyright © 1997 American Chemical Society

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    †

     Department of Soil Science and Plant Nutrition, University of Florence.

    ‡

     Department of Chemistry, University of Florence.

    §

     European Molecular Biology Laboratory.

    ‖

     Göteborg University.

    *

    In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

    ✗

     Abstract published in Advance ACS Abstracts, October 1, 1997.

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    This article is cited by 41 publications.

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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 1997, 119, 45, 11023–11027
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja9715399
    Published November 12, 1997
    Copyright © 1997 American Chemical Society
    Request reuse permissions

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