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

De Araujo, AD; Herzig, V; Windley, MJ; Dziemborowicz, S; Mobli, M; Nicholson, GM; Alewood, PF; King, GF

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

De Araujo, AD Herzig, V Windley, MJ Dziemborowicz, S Mobli, M Nicholson, GM

Alewood, PF King, GF

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Publication Type:: Journal Article
Citation:: Antioxidants and Redox Signaling, 2013, 19 (16), pp. 1976 - 1980
Issue Date:: 2013-12-01

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Field	Value	Language
dc.contributor.author	De Araujo, AD	en_US
dc.contributor.author	Herzig, V	en_US
dc.contributor.author	Windley, MJ	en_US
dc.contributor.author	Dziemborowicz, S	en_US
dc.contributor.author	Mobli, M	en_US
dc.contributor.author	Nicholson, GM https://orcid.org/0000-0002-4277-4296	en_US
dc.contributor.author	Alewood, PF	en_US
dc.contributor.author	King, GF	en_US
dc.date.issued	2013-12-01	en_US
dc.identifier.citation	Antioxidants and Redox Signaling, 2013, 19 (16), pp. 1976 - 1980	en_US
dc.identifier.issn	1523-0864	en_US
dc.identifier.uri	http://hdl.handle.net/10453/27916
dc.description.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. © Mary Ann Liebert, Inc.	en_US
dc.relation.ispartof	Antioxidants and Redox Signaling	en_US
dc.relation.isbasedon	10.1089/ars.2013.5365	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Disulfides	en_US
dc.subject.mesh	Cysteine	en_US
dc.subject.mesh	Proteins	en_US
dc.subject.mesh	Protein Structure, Secondary	en_US
dc.subject.mesh	Protein Folding	en_US
dc.subject.mesh	Oxidation-Reduction	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.title	Do vicinal disulfide bridges mediate functionally important redox transformations in proteins?	en_US
dc.type	Journal Article
utslib.citation.volume	16	en_US
utslib.citation.volume	19	en_US
utslib.for	1101 Medical Biochemistry and Metabolomics	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	1115 Pharmacology and Pharmaceutical Sciences	en_US
dc.location.activity	Melbourne, AUSTRALIA
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
pubs.organisational-group	/University of Technology Sydney/Students
utslib.copyright.status	closed_access
pubs.issue	16	en_US
pubs.publication-status	Published	en_US
pubs.volume	19	en_US

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. © Mary Ann Liebert, Inc.

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http://hdl.handle.net/10453/27916