Manganese Proteins with Mono- & Dinuclear Sites
Published Online: 15 MAR 2006
Copyright © 2006 John Wiley & Sons, Ltd
Encyclopedia of Inorganic Chemistry
How to Cite
Penner-Hahn, J. E. 2006. Manganese Proteins with Mono- & Dinuclear Sites. Encyclopedia of Inorganic Chemistry. .
- Published Online: 15 MAR 2006
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.
- xylose isomerase;
- glutamine synthetase;
- phosphoglycerate mutase;
- superoxide dismutase;
- oxalate metabolism;