JBIC Journal of Biological Inorganic Chemistry

, Volume 19, Issue 1, pp 1–15

Peroxomanganese complexes as an aid to understanding redox-active manganese enzymes

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DOI: 10.1007/s00775-013-1067-4

Cite this article as:
Leto, D.F. & Jackson, T.A. J Biol Inorg Chem (2014) 19: 1. doi:10.1007/s00775-013-1067-4

Abstract

Over the past 7 years, there have been a significant number of studies describing the structural and electronic properties, as well as the chemical reactivity, of synthetic peroxomanganese adducts. Many redox-active manganese enzymes, including manganese-containing superoxide dismutases, extradiol catechol dioxygenases, and ribonucleotide reductases, are proposed to feature peroxomanganese intermediates in their catalytic cycles. The recent efforts to model these intermediates using synthetic complexes have thus provided a strong complement to mechanistic studies of the enzymes. This review provides both a summary and a perspective of work in this area, with an emphasis on the relationship between geometric and electronic structure and chemical reactivity for η2-peroxomanganese(III) and η1-alkylperoxomanganese(III) adducts.

Keywords

Manganese Peroxo Bonding Reactivity Spectroscopy 

Copyright information

© SBIC 2013

Authors and Affiliations

  1. 1.Department of Chemistry and Center for Environmentally Beneficial CatalysisUniversity of KansasLawrenceUSA