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Do vicinal disulfide bridges mediate functionally important redox transformations in proteins?
Journal article   Peer reviewed

Do vicinal disulfide bridges mediate functionally important redox transformations in proteins?

A D De Araujo, Volker Herzig, M J Windley, S Dziemborowicz, M Mobli, G M Nicholson, P F Alewood and G F King
Antioxidants and Redox Signaling, Vol.19(16), pp.1976-1980
2013
url
https://doi.org/10.1089/ars.2013.5365View
Published Version

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.

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