Journal
ANTIOXIDANTS & REDOX SIGNALING
Volume 19, Issue 16, Pages 1976-1980Publisher
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2013.5365
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Funding
- Australian Research Council [DP1095728]
- Australian Research Council [DP1095728] Funding Source: Australian Research Council
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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.
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