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Title 

Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path

Authors 

Cheolju LeeSoon Mi LeeP MukhopadhyaySeung-Jun KimSang Chul LeeW S AhnM H YuG StorzSeong Eon Ryu

Publisher 

Nature Publishing Group

Issue Date 

2004

Citation 

Nature Structural Biology, vol. 11, no. 12, pp. 1179-1185

Keywords 

disulfideDNA binding proteinescherichia coli proteinoxidizing agentoxyR protein, E colitranscription factortryptophanureachemical structureescherichia coli

Abstract 

The Escherichia coli OxyR transcription factor is activated by cellular hydrogen peroxide through the oxidation of reactive cysteines. Although there is substantial evidence for specific disulfide bond formation in the oxidative activation of OxyR, the presence of the disulfide bond has remained controversial. By mass spectrometry analyses and in vivo labeling assays we found that oxidation of OxyR in the formation of a specific disulfide bond between Cys199 and Cys208 in the wild-type protein. In addition, using time-resolved kinetic analyses, we determined that OxyR activation occurs at a rate of 9.7 s(-1). The disulfide bond-mediated conformation switch results in a metastable form that is locally strained by approximately 3 kcal mol(-1). On the basis of these observations we conclude that OxyR activation requires specific disulfide bond formation and that the rapid kinetic reaction path and conformation strain, respectively, drive the oxidation and reduction of OxyR.

ISSN 

1072-8368

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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