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Article: Redox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude

TitleRedox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude
Authors
Issue Date2012
Citation
Chemical Communications, 2012, v. 48, n. 35, p. 4217-4219 How to Cite?
AbstractThe same non-covalent interactions previously found to affect the redox potential (E m) of the mononuclear T1 Cu protein azurin (Az) are shown to also fine-tune the E m of the dinuclear Cu A center in the same Az protein scaffold. The effects of these mutations are in the same direction but with smaller magnitude in the Cu A site, due to dissipation of the effects by the dinuclear Cu A center. © 2012 The Royal Society of Chemistry.
Persistent Identifierhttp://hdl.handle.net/10722/219663
ISSN
2015 Impact Factor: 6.567
2015 SCImago Journal Rankings: 2.771

 

DC FieldValueLanguage
dc.contributor.authorNew, Siu Yee-
dc.contributor.authorMarshall, Nicholas M.-
dc.contributor.authorHor, T. S Andy-
dc.contributor.authorXue, Feng-
dc.contributor.authorLu, Yi-
dc.date.accessioned2015-09-23T02:57:40Z-
dc.date.available2015-09-23T02:57:40Z-
dc.date.issued2012-
dc.identifier.citationChemical Communications, 2012, v. 48, n. 35, p. 4217-4219-
dc.identifier.issn1359-7345-
dc.identifier.urihttp://hdl.handle.net/10722/219663-
dc.description.abstractThe same non-covalent interactions previously found to affect the redox potential (E m) of the mononuclear T1 Cu protein azurin (Az) are shown to also fine-tune the E m of the dinuclear Cu A center in the same Az protein scaffold. The effects of these mutations are in the same direction but with smaller magnitude in the Cu A site, due to dissipation of the effects by the dinuclear Cu A center. © 2012 The Royal Society of Chemistry.-
dc.languageeng-
dc.relation.ispartofChemical Communications-
dc.titleRedox tuning of two biological copper centers through non-covalent interactions: Same trend but different magnitude-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1039/c2cc30901g-
dc.identifier.pmid22441412-
dc.identifier.scopuseid_2-s2.0-84859319516-
dc.identifier.volume48-
dc.identifier.issue35-
dc.identifier.spage4217-
dc.identifier.epage4219-
dc.identifier.eissn1364-548X-

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