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Reduction Potential Tuning at a Type 1 Copper Site Does Not Compromise Electron Transfer Reactivity

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Contribution from the Institute for Cell and Molecular Biosciences, Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne, NE2 4HH, UK
Cite this: J. Am. Chem. Soc. 2005, 127, 47, 16453–16459
Publication Date (Web):November 4, 2005
https://doi.org/10.1021/ja054426v
Copyright © 2005 American Chemical Society

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    Abstract

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    Type 1 (T1) copper sites promote biological electron transfer (ET) and typically possess a weakly coordinated thioether sulfur from an axial Met [Cu(II)−Sδ ∼ 2.6 to 3.3 Å] along with the conserved His2Cys equatorial ligands. A strong axial bond [Cu(II)−Oε1 ∼ 2.2 Å] is sometimes provided by a Gln (as in the stellacyanins), and the axial ligand can be absent (a Val, Leu or Phe in the axial position) as in ceruloplasmin, Fet3p, fungal laccases and some plantacyanins (PLTs). Cucumber basic protein (CBP) is a PLT which has a relatively short Cu(II)−S(Met89) axial bond (2.6 Å). The Met89Gln variant of CBP has an electron self-exchange (ESE) rate constant (kese, a measure of intrinsic ET reactivity) ∼7 times lower than that of the wild-type protein. The Met89Val mutation to CBP results in a 2-fold increase in kese. As the axial interaction decreases from strong Oε1 of Gln to relatively weak Sδ of Met to no ligand (Val), ESE reactivity is therefore enhanced by ∼1 order of magnitude while the reduction potential increases by ∼350 mV. The variable coordination position at this ubiquitous ET site provides a mechanism for tuning the driving force to optimize ET with the correct partner without significantly compromising intrinsic reactivity. The enhanced reactivity of a three-coordinate T1 copper site will facilitate intramolecular ET in fungal laccases and Fet3p.

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    A table showing the primers used to synthesize and amplify the artificial coding region for CBP, and figures showing comparisons of UV/vis and EPR spectra of WT, Met89Gln, and Met89Val CBP. This material is available free of charge via the Internet at http://pubs.acs.org.

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