Journal article
Do vicinal disulfide bridges mediate functionally important redox transformations in proteins?
Antioxidants and Redox Signaling, Vol.19(16), pp.1976-1980
2013
Abstract
Vicinal disulfide bridges, in which a disulfide bond is formed between adjacent cysteine residues, constitute an unusual but expanding class of potential allosteric disulfides. Although vicinal disulfide rings (VDRs) are relatively uncommon, they have proven to be functionally critical in almost all proteins in which they have been discovered. However, it has proved difficult to test whether these sterically constrained disulfides participate in functionally important redox transformations. We demonstrate that chemical replacement of VDRs with dicarba or diselenide bridges can be used to assess whether VDRs function as allosteric disulfides. Our approach leads to the hypothesis that not all VDRs participate in functionally important redox reactions. Antioxid. Redox Signal. 19, 1976-1980.
Details
- Title
- Do vicinal disulfide bridges mediate functionally important redox transformations in proteins?
- Authors
- A D De Araujo (Author) - University of QueenslandVolker Herzig (Author) - University of QueenslandM J Windley (Author) - University of Technology, SydneyS Dziemborowicz (Author) - University of Technology, SydneyM Mobli (Author) - University of QueenslandG M Nicholson (Author) - University of Technology, SydneyP F Alewood (Author) - University of QueenslandG F King (Author) - University of Queensland
- Publication details
- Antioxidants and Redox Signaling, Vol.19(16), pp.1976-1980
- Publisher
- Mary Ann Liebert, Inc. Publishers
- Date published
- 2013
- DOI
- 10.1089/ars.2013.5365
- ISSN
- 1523-0864
- Organisation Unit
- School of Science and Engineering - Legacy; University of the Sunshine Coast, Queensland; School of Science, Technology and Engineering; Centre for Bioinnovation
- Language
- English
- Record Identifier
- 99451333302621
- Output Type
- Journal article
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- Domestic collaboration
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- Biochemistry & Molecular Biology
- Endocrinology & Metabolism
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