Standard Article

Manganese Proteins with Mono- & Dinuclear Sites

  1. James E. Penner-Hahn

Published Online: 15 DEC 2011

DOI: 10.1002/9781119951438.eibc0122

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Penner-Hahn, J. E. 2011. Manganese Proteins with Mono- & Dinuclear Sites. Encyclopedia of Inorganic and Bioinorganic Chemistry. .

Author Information

  1. The University of Michigan, Ann Arbor, MI, USA

Publication History

  1. Published Online: 15 DEC 2011

This is not the most recent version of the article. View current version (23 DEC 2015)

Abstract

Although manganese is not as widely recognized as iron and copper, it nevertheless plays an essential role in several key biological processes. Consequently, manganese concentrations are tightly regulated in most cells. Several Mn-specific transporters have been identified and a novel Mn-regulatory protein has been characterized. Manganese-activated enzymes are proteins that have relatively weak affinities for Mn; in many cases these are isolated without any metal bound. Manganese-activated enzymes are especially important in hydrolytic reactions, and appear, in at least some cases, to have physiologically significant changes in activity that respond to changes in Mn concentration. The best characterized Mn proteins are redox-active enzymes, where Mn typically cycles between the MnII and MnIII oxidation states, although some MnIV-containing species are known.

Keywords:

  • homeostasis;
  • xylose isomerase;
  • glutamine synthetase;
  • phosphoglycerate mutase;
  • superoxide dismutase;
  • dioxygenase;
  • oxalate metabolism;
  • arginase;
  • catalase