Fe-S proteins in sensing and regulatory functions

H Beinert; P J Kiley

doi:10.1016/S1367-5931(99)80027-1

Fe-S proteins in sensing and regulatory functions

Curr Opin Chem Biol. 1999 Apr;3(2):152-7. doi: 10.1016/S1367-5931(99)80027-1.

Authors

H Beinert¹, P J Kiley

Affiliation

¹ Institute for Enzyme Research, Graduate School, Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, 1710 University Avenue, Madison, WI 53705, USA. hbeinert@facstaff.wisc.edu

PMID: 10226040
DOI: 10.1016/S1367-5931(99)80027-1

Abstract

In the past five to ten years, it has become increasingly apparent that the function of Fe-S clusters is not limited to electron transfer, a function implicit in their discovery. We now know that the vulnerability of these structures to oxidative destruction is used by nature in sensing O2, iron, and possibly also nitric oxide. Changes in the oxidation state of Fe-S clusters can also serve as a reversible switch.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review

MeSH terms

Bacterial Proteins / physiology
Escherichia coli / metabolism
Iron-Sulfur Proteins / physiology*
Oxidative Stress

Substances

Bacterial Proteins
Iron-Sulfur Proteins

Grants and funding

GM45844/GM/NIGMS NIH HHS/United States