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Disulfides as redox switches : from molecular mechanisms to functional significance

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journal contribution
posted on 2010-01-01, 00:00 authored by Merridee Wouters, S Fan, N Haworth
The molecular mechanisms underlying thiol-based redox control are poorly defined. Disulfide bonds between Cys residues are commonly thought to confer extra rigidity and stability to their resident protein, forming a type of proteinaceous spot weld. Redox biologists have been redefining the role of disulfides over the last 30–40 years. Disulfides are now known to form in the cytosol under conditions of oxidative stress. Isomerization of extracellular disulfides is also emerging as an important regulator of protein function. The current paradigm is that the disulfide proteome consists of two subproteomes: a structural group and a redox-sensitive group. The redoxsensitive group is less stable and often associated with regions of stress in protein structures. Some characterized redox-active disulfides are the helical CXXC motif, often associated with thioredoxin-fold proteins; and forbidden disulfides, a group of metastable disulfides that disobey elucidated rules of protein stereochemistry. Here we discuss the role of redox-active disulfides as switches in proteins.

History

Journal

Antioxidants and redox signalling

Volume

12

Issue

1

Pagination

53 - 91

Publisher

Mary Ann Liebert Inc. Publishers

Location

New Rochelle, N. Y.

ISSN

1523-0864

eISSN

1557-7716

Language

eng

Notes

This is a copy of an article published in the Antioxidants and Redox Signaling © 2010 Mary Ann Liebert, Inc.; Antioxidants and Redox Signaling is available online at: http://online.liebertpub.com.

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2010, Mary Ann Liebert Publishers

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