Fe-S proteins in sensing and regulatory functions

被引：167

作者：

Beinert, H

Kiley, PJ

机构：

[1] Univ Wisconsin, Grad Sch, Inst Enzyme Res, Madison, WI 53705 USA

[2] Univ Wisconsin, Coll Agr & Life Sci, Dept Biochem, Madison, WI 53705 USA

[3] Univ Wisconsin, Sch Med, Dept Biomol Chem, Madison, WI 53706 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 1999年 / 3卷 / 02期

关键词：

D O I：

10.1016/S1367-5931(99)80027-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 O-2, iron, and possibly also nitric oxide. Changes in the oxidation state of Fe-S clusters can also serve as a reversible switch.

引用

页码：152 / 157

页数：6

共 59 条

[1] An all-ferrous state of the Fe protein of nitrogenase -: Interaction with nucleotides and electron transfer to the MoFe protein [J].