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Spectroscopic and computational investigation of three Cys-to-Ser mutants of nickel superoxide dismutase: insight into the roles played by the Cys2 and Cys6 active-site residues

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Abstract

Nickel-dependent superoxide dismutase (NiSOD) is a member of a class of metalloenzymes that protect aerobic organisms from the damaging superoxide radical (O2 ·−). A distinctive and fascinating feature of NiSOD is the presence of active-site nickel–thiolate interactions involving the Cys2 and Cys6 residues. Mutation of one or both Cys residues to Ser prevents catalysis of O2 ·−, demonstrating that both residues are necessary to support proper enzymatic activity (Ryan et al., J Biol Inorg Chem, 2010). In this study, we have employed a combined spectroscopic and computational approach to characterize three Cys-to-Ser (Cys → Ser) mutants (C2S, C6S, and C2S/C6S NiSOD). Similar electronic absorption and magnetic circular dichroism spectra are observed for these mutants, indicating that they possess nearly identical active-site geometric and electronic structures. These spectroscopic data also reveal that the Ni2+ ion in each mutant adopts a high-spin (S = 1) configuration, characteristic of a five- or six-coordinate ligand environment, as opposed to the low-spin (S = 0) configuration observed for the four-coordinate Ni2+ center in the native enzyme. An analysis of the electronic absorption and magnetic circular dichroism data within the framework of density functional theory computations performed on a series of five- and six-coordinate C2S/C6S NiSOD models reveals that the active site of each Cys → Ser mutant possesses an essentially six-coordinate Ni2+ center with a rather weak axial bonding interaction. Factors contributing to the lack of catalytic activity displayed by the Cys → Ser NiSOD mutants are explored.

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Abbreviations

B3LYP:

Becke’s three-parameter hybrid functional for exchange combined with the Lee–Yang–Par correlation functional

CD:

Circular dichroism

Cys → Ser:

Cysteine to serine

DFT:

Density functional theory

EPR:

Electron paramagnetic resonance

EXAFS:

Extended X-ray absorption fine structure

HOMO:

Highest occupied molecular orbital

INDO/S-CI:

Intermediate neglect of differential overlap/spectroscopic parameterization with configuration interaction

LF:

Ligand field

MCD:

Magnetic circular dichroism

MO:

Molecular orbital

NiSOD:

Nickel-dependent superoxide dismutase

NiSODox :

Oxidized nickel-dependent superoxide dismutase

NiSODred :

Reduced nickel-dependent superoxide dismutase

SOD:

Superoxide dismutase

TD-DFT:

Time-dependent density functional theory

Tris:

Tris(hydroxymethyl)aminomethane

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Acknowledgments

This work was supported by the National Institutes of Health (Grant GM 64631 to T.C.B.), the University of Wisconsin Chemical Biology Interface Training Grant from the National Institutes of Health (Grant T32 GM008505 to O.E.J.), and the National Science Foundation (Grant CHE-0809188 to M.J.M).

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Authors and Affiliations

  1. Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA

    Olivia E. Johnson & Thomas C. Brunold

  2. Department of Chemistry, University of Massachusetts at Amherst, 104 Lederle Graduate Research Tower A, 710 North Pleasant Street, Amherst, MA, 01003, USA

    Kelly C. Ryan & Michael J. Maroney

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  1. Olivia E. Johnson
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Correspondence to Thomas C. Brunold.

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Johnson, O.E., Ryan, K.C., Maroney, M.J. et al. Spectroscopic and computational investigation of three Cys-to-Ser mutants of nickel superoxide dismutase: insight into the roles played by the Cys2 and Cys6 active-site residues. J Biol Inorg Chem 15, 777–793 (2010). https://doi.org/10.1007/s00775-010-0641-2

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