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James Whittaker Institute of Environmental Health

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James Whittaker

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Non-heme manganese catalase - The 'other' catalase

James W. Whittaker

(Profiled Author: James Whittaker)

Archives of Biochemistry and Biophysics. 2012;525(2):111-120.

Abstract

Non-heme manganese catalases are widely distributed over microbial life and represent an environmentally important alternative to heme-containing catalases in antioxidant defense. Manganese catalases contain a binuclear manganese complex as their catalytic active site rather than a heme, and cycle between Mn 2(II,II) and Mn 2(III,III) states during turnover. X-ray crystallography has revealed the key structural elements of the binuclear manganese active site complex that can serve as the starting point for computational studies on the protein. Four manganese catalase enzymes have been isolated and characterized, and the enzyme appears to have a broad phylogenetic distribution including both bacteria and archae. More than 100 manganese catalase genes have been annotated in genomic databases, although the assignment of many of these putative manganese catalases needs to be experimentally verified. Iron limitation, exposure to low levels of peroxide stress, thermostability and cyanide resistance may provide the biological and environmental context for the occurrence of manganese catalases. © 2012 Elsevier Inc. All rights reserved.


PMID: 22198285     PMCID: PMC3328634    

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