Oxidation and Loss of Heme in Soluble Guanylyl Cyclase from Manduca sexta

被引：49

作者：

Fritz, Bradley G. ^{[1
]}

Hu, Xiaohui ^{[1
]}

Brailey, Jacqueline L. ^{[1
]}

Berry, Robert E. ^{[1
]}

Walker, F. Ann ^{[1
]}

Montfort, William R. ^{[1
]}

机构：

[1] Univ Arizona, Dept Chem & Biochem, Tucson, AZ 85721 USA

来源：

BIOCHEMISTRY | 2011年 / 50卷 / 26期

基金：

美国国家卫生研究院;

关键词：

LIGAND-BINDING; NO; ACTIVATION; DISTORTION; COMPLEXES; CO; STABILIZATION; DEGRADATION; PROTEIN;

D O I：

10.1021/bi200794c

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

Oxidation and loss of heme in soluble guanylyl/guanylate cyclase (sGC), the nitric oxide receptor, is thought to be a major contributor to cardiovascular disease and is the target of compounds BAY 58-2667 and HMR1766. Using spectroelectrochemical titration, we found a truncated sGC to be highly stable in the ferrous state (234 mV) and to bind ferrous heme tightly even in the presence of NO, despite the NO-induced release of the proximal histidine. In contrast, oxidized sGC readily loses ferric heme to myoglobin (0.47 +/- 0.02 h(-1)). Peroxynitrite, the presumed cellular oxidant, readily oxidizes sGC in 5 mM glutathione.

引用

页码：5813 / 5815

页数：3

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