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Download Hi-Res ImageDownload to MS-PowerPointCite This:Inorg. Chem. 2005, 44, 9, 3311-3320
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Copper−Zinc Superoxide Dismutase:  Theoretical Insights into the Catalytic Mechanism

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Department of Physics, Stockholm University, S-106 91 Stockholm, Sweden
Cite this: Inorg. Chem. 2005, 44, 9, 3311–3320
Publication Date (Web):April 7, 2005
https://doi.org/10.1021/ic050018g
Copyright © 2005 American Chemical Society
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Abstract

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The mechanism for the toxic superoxide radical disproportionation to molecular oxygen and hydrogen peroxide by copper−zinc superoxide dismutase (CuZnSOD) has been studied using the B3LYP hybrid density functional. On the basis of the X-ray structure of the enzyme, the molecular system investigated includes the first-shell protein ligands of the two metal centers as well as the second-shell ligand Asp122. The substrates of the model reaction are two superoxide radical anions, approaching the copper center at the beginning of two half-reactions:  the first part of the catalytic cycle involving Cu+ oxidation and the second part reducing Cu2 + back to its initial state. The quantitative free energy profile of the reaction is obtained and discussed in connection with the experimental data on the reduction potentials and CuZnSOD kinetics. The optimized structures are analyzed and compared to the experimental ones. The two transition states alternate the protonation state of His61 and correspond to histidine Cu-His61-Zn bridge rupture/reformation. Modifications applied to the initial model allow the importance of Asp122 for catalysis to be estimated.

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GIF file showing the first transition state TS1 of the CuZnSOD mechanism, a visualized vibration that depicts the Cu-His61-Zn bridge protonation and corresponds to the imaginary frequency of −266 cm-1; GIF file showing the second transition state TS2 of the CuZnSOD mechanism, a visualized vibration that depicts the Cu-His61-Zn bridge re-formation and corresponds to the imaginary frequency of −134 cm-1; chart depicting two metastable complexes (1‘ and 6‘, respectively) in which •OOH/H2O2 weakly bind to Cu2+/Cu2+ model clusters. This material is available free of charge via the Internet at http://pubs.acs.org.

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