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Thiol oxidase ability of copper ion is specifically retained upon chelation by aldose reductase

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Abstract

Bovine lens aldose reductase is susceptible to a copper-mediated oxidation, leading to the generation of a disulfide bridge with the concomitant incorporation of two equivalents of the metal and inactivation of the enzyme. The metal complexed by the protein remains redox active, being able to catalyse the oxidation of different physiological thiol compounds. The thiol oxidase activity displayed by the enzymatic form carrying one equivalent of copper ion (Cu1-AR) has been characterized. The efficacy of Cu1-AR in catalysing thiol oxidation is essentially comparable to the free copper in terms of both thiol concentration and pH effect. On the contrary, the two catalysts are differently affected by temperature. The specificity of the AR-bound copper towards thiols is highlighted with Cu1-AR being completely ineffective in promoting the oxidation of both low-density lipoprotein and ascorbic acid.

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Acknowledgements

This work was supported by Pisa University, PRA 2015. We are indebted to Dr. G. Pasqualetti and Dr. R. Di Sacco (veterinary staff of Consorzio Macelli S. Miniato, Pisa) for their valuable co-operation in the bovine lenses collection.

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Authors and Affiliations

  1. Biochemistry Unit, Department of Biology, University of Pisa, via San Zeno, 51, 56123, Pisa, Italy

    Francesco Balestri, Roberta Moschini, Mario Cappiello, Umberto Mura & Antonella Del-Corso

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  1. Francesco Balestri
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  2. Roberta Moschini
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Correspondence to Antonella Del-Corso.

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Balestri, F., Moschini, R., Cappiello, M. et al. Thiol oxidase ability of copper ion is specifically retained upon chelation by aldose reductase. J Biol Inorg Chem 22, 559–565 (2017). https://doi.org/10.1007/s00775-017-1447-2

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  • DOI: https://doi.org/10.1007/s00775-017-1447-2

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