谷胱甘肽复合铁-硫中心。
Glutathione complexed Fe-S centers.
机构信息
Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Avenue, Columbus, Ohio 43210, USA.
出版信息
J Am Chem Soc. 2012 Jul 4;134(26):10745-8. doi: 10.1021/ja302186j. Epub 2012 Jun 21.
Abstract
Glutathione (γ-glutamyl-cysteinyl-glycine, GSH) is a major thiol-containing peptide with cellular levels of up to 10 mM. (1) Several recent reports have demonstrated glutaredoxins (Grx) to form [Fe(2)S(2)] cluster-bridged dimers, where glutathione provides two exogenous thiol ligands, and have implicated such species in cellular iron sulfur cluster biosynthesis. We report the finding that glutathione alone can coordinate and stabilize an [Fe(2)S(2)] cluster under physiological conditions, with optical, redox, Mössbauer, and NMR characteristics that are consistent with a Fe(2)S(2)(4) composition. The Fe-S assembly protein ISU catalyzes formation of Fe(2)S(2)(4) from iron and sulfide ions in the presence of glutathione, and the [Fe(2)S(2)] core undergoes reversible exchange between apo ISU and free glutathione.
摘要
谷胱甘肽（γ-谷氨酰半胱氨酸甘氨酸，GSH）是一种主要的含巯基肽，细胞内水平高达 10mM。（1）最近的几项研究表明，谷氧还蛋白（Grx）形成[Fe（2）S（2）]簇桥联二聚体，其中谷胱甘肽提供两个外源性巯基配体，并暗示这种物质参与细胞铁硫簇生物合成。我们报告发现，在生理条件下，谷胱甘肽本身可以协调和稳定[Fe（2）S（2）]簇，其光学、氧化还原、穆斯堡尔和 NMR 特征与[Fe（2）S（2）]（GS）（4）组成一致。铁硫组装蛋白 ISU 在谷胱甘肽存在的情况下，催化铁和硫化物离子形成[Fe（2）S（2）]（GS）（4），并且[Fe（2）S（2）]核心在脱辅基 ISU 和游离谷胱甘肽之间进行可逆交换。
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