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Spectroscopic and Density Functional Theory Studies of the Blue−Copper Site in M121SeM and C112SeC Azurin:  Cu−Se Versus Cu−S Bonding

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    Spectroscopic and Density Functional Theory Studies of the Blue−Copper Site in M121SeM and C112SeC Azurin:  Cu−Se Versus Cu−S Bonding
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    Department of Chemistry, Stanford University, Stanford, California 94305, Stanford Synchrotron Radiation Laboratory, Stanford Linear Accelerator Center, Stanford University, Stanford, California 94309, and Department of Chemistry and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2008, 130, 12, 3866–3877
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    https://doi.org/10.1021/ja076495a
    Published March 4, 2008
    Copyright © 2008 American Chemical Society
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    Abstract

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    S K-edge X-ray absorption, UV−vis absorption, magnetic circular dichroism (MCD), and resonance Raman spectroscopies are used to investigate the electronic structure differences among WT, M121SeM, and C112SeC Pseudomonas aeruginosa (P.a) azurin. A comparison of S K-edge XAS of WT and M121SeM azurin and a CuII−thioether model complex shows that the 38% S character in the ground state wave function of the blue−copper (BC) sites solely reflects the Cu−SCys bond. Resonance Raman (rR) data on WT and C112SeC azurin give direct evidence for the kinematic coupling between the Cu−SCys stretch and the cysteine deformation modes in WT azurin, which leads to multiple features in the rR spectrum of the BC site. The UV−vis absorption and MCD data on WT, M121SeM, and C112SeC give very similar C0/D0 ratios, indicating that the C-term MCD intensity mechanism involves Cu-centered spin−orbit coupling (SOC). The spectroscopic data combined with density functional theory (DFT) calculations indicate that SCys and SeCys have similar covalent interactions with Cu at their respective bond lengths of 2.1 and 2.3 Å. This reflects the similar electronegativites of S and Se in the thiolate/selenolate ligand fragment and explains the strong spectroscopic similarities between WT and C112SeC azurin.

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    †

     Stanford University.

    ‡

     Current address:  Center for Catalysis Research and Innovation, Department of Chemistry, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada.

    ⊥

     University of Illinois at Urbana−Champaign.

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

    §

     Stanford Linear Accelerator Center, Stanford University.

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    The structure of CuL1; overlay of UV−vis absorption and MCD spectra of WT, M121SeM, and C112SeC azurin; geometry-optimized structure and xyz coordinates of [Cu(tpz)(SC6F5)] and [Cu(tpz)(SeC6F5)] and the LCu+ and SC6F5- interaction energy diagram; and complete ref 30. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cite this: J. Am. Chem. Soc. 2008, 130, 12, 3866–3877
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja076495a
    Published March 4, 2008
    Copyright © 2008 American Chemical Society
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