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Nat Chem. 2018 Dec;10(12):1207-1212. doi: 10.1038/s41557-018-0137-1. Epub 2018 Oct 1.

Superoxide dismutase activity enabled by a redox-active ligand rather than metal.

Author information

1
Department of Chemistry and Biochemistry, Auburn University, Auburn, AL, USA.
2
Department of Chemistry and Pharmacy, University of Erlangen-Nürnberg, Erlangen, Germany.
3
Department of Anatomy, Physiology, and Pharmacology, College of Veterinary Medicine, Auburn University, Auburn, AL, USA.
4
Department of Chemistry and Pharmacy, University of Erlangen-Nürnberg, Erlangen, Germany. ivana.ivanovic-burmazovic@fau.de.
5
Department of Chemistry and Biochemistry, Auburn University, Auburn, AL, USA. crgoldsmith@auburn.edu.

Abstract

Reactive oxygen species are integral to many physiological processes. Although their roles are still being elucidated, they seem to be linked to a variety of disorders and may represent promising drug targets. Mimics of superoxide dismutases, which catalyse the decomposition of O2•- to H2O2 and O2, have traditionally used redox-active metals, which are toxic outside of a tightly coordinating ligand. Purely organic antioxidants have also been investigated but generally require stoichiometric, rather than catalytic, doses. Here, we show that a complex of the redox-inactive metal zinc(II) with a hexadentate ligand containing a redox-active quinol can catalytically degrade superoxide, as demonstrated by both reactivity assays and stopped-flow kinetics studies of direct reactions with O2- and the zinc(II) complex. The observed superoxide dismutase catalysis has an important advantage over previously reported work in that it is hastened, rather than impeded, by the presence of phosphate, the concentration of which is high under physiological conditions.

PMID:
30275506
DOI:
10.1038/s41557-018-0137-1

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