title: Do vicinal disulfide bridges mediate functionally important redox transformations in proteins?
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.
authors: 1 Institute for Molecular Bioscience, The University of Queensland , St. Lucia, Australia .
authors: Aline Dantas
authors: AD
authors: de Araujo
authors: Volker
authors: V
authors: Herzig
authors: Monique J
authors: MJ
authors: Windley
authors: Sławomir
authors: S
authors: Dziemborowicz
authors: Mehdi
authors: M
authors: Mobli
authors: Graham M
authors: GM
authors: Nicholson
authors: Paul F
authors: PF
authors: Alewood
authors: Glenn F
authors: GF
authors: King
mesh_terms: D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D004220:Disulfides; D011506:Proteins; D003545:Cysteine
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