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    π-Interaction Tuning of the Active Site Properties of Metalloproteins
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    Institute for Cell and Molecular Biosciences, Medical School, Newcastle University, Newcastle upon Tyne, NE2 4HH, U.K., UCD School of Biomolecular and Biomedical Science, Conway Institute, University College Dublin, Belfield, Dublin 4, Ireland, School of Natural Sciences (Chemistry), Bedson Building, Newcastle University, Newcastle upon Tyne, NE1 7RU, U.K., and Institute of Applied Beam Science, Ibaraki University, Mito, Ibaraki 310-8512, Japan
    [email protected]
    †Medical School, Newcastle University.
    ‡University College Dublin.
    §Bedson Building, Newcastle University.
    ∥Ibaraki University.
    ⊥Current address: Department of Biological Chemistry, John Innes Centre, Norwich, NR4 7UH, and School of Chemical Sciences and Pharmacy, University of East Anglia, Earlham Road, Norwich, NR4 7TJ, U.K.
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2008, 130, 46, 15420–15428
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    https://doi.org/10.1021/ja8038135
    Published October 21, 2008
    Copyright © 2008 American Chemical Society
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    Abstract

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    The influence of π-interactions with a His ligand have been investigated in a family of copper-containing redox metalloproteins. The Met16Phe and Met16Trp pseudoazurin, and Leu12Phe spinach and Leu14Phe Phormidium laminosum plastocyanin variants possess active-site π-contacts between the introduced residue and His81 and His87/92 respectively. The striking overlap of the side chain of Phe16 in the Met16Phe variant and that of Met16 in wild type pseudoazurin identifies that this position provides an important second coordination sphere interaction in both cases. His-ligand protonation and dissociation from Cu(I) occurs in the wild type proteins resulting in diminished redox activity, providing a [H+]-driven switch for regulating electron transfer. The introduced π-interaction has opposing effects on the pKa for the His ligand in pseudoazurin and plastocyanin due to subtle differences in the π-contact, stabilizing the coordinated form of pseudoazurin whereas in plastocyanin protonation and dissociation is favored. Replacement of Pro36, a residue that has been suggested to facilitate structural changes upon His ligand protonation, with a Gly, has little effect on the pKa of His87 in spinach plastocyanin. The mutations at Met16 have a significant influence on the reduction potential of pseudoazurin. Electron self-exchange is enhanced, whereas association with the physiological partner, nitrite reductase, is only affected by the Met16Phe mutation, but kcat is halved in both the Met16Phe and Met16Trp variants. Protonation of the His ligand is the feature most affected by the introduction of a π-interaction.

    Copyright © 2008 American Chemical Society

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    Supporting Information

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    Detailed materials and methods and spectroscopic and electron self-exchange rate constant results, as well as Tables comparing the active site structures of WT and Met16Phe PAZ and also WT and Leu14Phe P. laminosum PC. Also included are figures showing UV/vis and EPR spectra, the dependence on pH of the chemical shift values of His ligand resonances in WT, Met16Phe and Met16Trp PAZ and also in WT and Leu14Phe P. laminosum PC, plots of T1−1 against [Cu(II)] for His ligand resonances in Met16Phe PAZ and Lineweaver−Burk plots for the oxidation of Cu(I) WT, and Met16Phe and Met16Trp PAZ by NIR. This material is available free of charge via the Internet at http://pubs.ac.org.

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    Cite this: J. Am. Chem. Soc. 2008, 130, 46, 15420–15428
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja8038135
    Published October 21, 2008
    Copyright © 2008 American Chemical Society
    Request reuse permissions

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