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Thioredoxin Ch1 of Chlamydomonas reinhardtii displays an unusual resistance toward one-electron oxidation.

作者信息

Sicard-Roselli Cécile, Lemaire Stéphane, Jacquot Jean-Pierre, Favaudon Vincent, Marchand Christophe, Houée-Levin Chantal

机构信息

Laboratoire de Chimie Physique, Université Paris XI, Orsay, France.

出版信息

Eur J Biochem. 2004 Sep;271(17):3481-7. doi: 10.1111/j.1432-1033.2004.04279.x.

DOI:10.1111/j.1432-1033.2004.04279.x
PMID:15317583
Abstract

To test thioredoxin resistance to oxidizing free radicals, we have studied the one-electron oxidation of wild-type thioredoxin and of two forms with the point mutations D30A and W35A, using azide radicals generated by gamma-ray or pulse radiolysis. The oxidation patterns of wild-type thioredoxin and D30A are similar. In these forms, Trp35 is the primary target and is 'repaired' by one-electron reduction; first by intramolecular electron transfer from tyrosine, and then from other residues. Conversely, during oxidation of W35A, Trp13 is poorly reactive. For all proteins, activity is conserved showing an unusual resistance toward oxidation.

摘要

相似文献

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