OXIDATION OF METHIONYL RESIDUES IN PROTEINS - TOOLS, TARGETS, AND REVERSAL

被引：754

作者：

VOGT, W

机构：

[1] Max Planck Institut für experimentelle Medizin, Göttingen

来源：

FREE RADICAL BIOLOGY AND MEDICINE | 1995年 / 18卷 / 01期

关键词：

METHIONINE OXIDATION; METHIONINE SULFOXIDE REDUCTION; PROTEIN; ACTIVATION/INACTIVATION BY MET OXIDATION; FREE RADICALS;

D O I：

10.1016/0891-5849(94)00158-G

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：

Methionine (Met) is one of the most readily oxidized amino acid constituents of proteins. It is attacked by H2O2, hydroxyl radicals, hypochlorite, chloramines, and peroxynitrite, ail these oxidants being produced in biological systems. The oxidation product, Met sulfoxide, can be reduced back to Met by Met sulfoxide reductase. Numerous proteins lose functional activity by Met oxidation. However, functional activation of proteins by Met oxidation has also been observed. Functional changes by Met oxidation in a given protein appear to have pathophysiological significance in some cases. Considering the reversibility of Met oxidation and the functional changes associated with the oxidation, it seems possible that Met oxidation/reduction in proteins may be one means to control homeostasis in biologicals systems.

引用

页码：93 / 105

页数：13

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