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Article: 1H NMR study of 2-methylimidazole binding to cytochrome c: A comprehensive investigation of the role of the methyl substituent on the ligand binding affinity and heme electronic structure in imidazole-cytochrome c complexes

Title1H NMR study of 2-methylimidazole binding to cytochrome c: A comprehensive investigation of the role of the methyl substituent on the ligand binding affinity and heme electronic structure in imidazole-cytochrome c complexes
Authors
Issue Date2001
Citation
Journal Of The Chemical Society, Dalton Transactions, 2001 n. 12, p. 1841-1845 How to Cite?
AbstractThe binding of 2-methylimidazole (2mim) to horse heart cytochrome c (hh cyt c) has been studied by NMR spectroscopy. Some proton resonances were assigned and the kinetic and thermodynamic parameters for the binding were presented. Based on its unique hyperfine shift pattern and the anomalous temperature dependence of the heme methyl resonances, the heme electronic structure was discussed and the orientation of the bound 2mim was estimated. With these data, a comprehensive comparison of imidazole (Him), 4-methylimidazole (4mim) and 2mim bound cyt c complexes was made on the ligand binding affinity and the heme electronic structure. Different properties in these ligand-cyt c complexes provide a useful lesson for the study of protein-small molecular interactions.
Persistent Identifierhttp://hdl.handle.net/10722/147458
ISSN
References
Errata

 

DC FieldValueLanguage
dc.contributor.authorYao, Yen_US
dc.contributor.authorQian, Cen_US
dc.contributor.authorWu, Yen_US
dc.contributor.authorHu, Jen_US
dc.contributor.authorTang, Wen_US
dc.date.accessioned2012-05-29T06:03:52Z-
dc.date.available2012-05-29T06:03:52Z-
dc.date.issued2001en_US
dc.identifier.citationJournal Of The Chemical Society, Dalton Transactions, 2001 n. 12, p. 1841-1845en_US
dc.identifier.issn1470-479Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/147458-
dc.description.abstractThe binding of 2-methylimidazole (2mim) to horse heart cytochrome c (hh cyt c) has been studied by NMR spectroscopy. Some proton resonances were assigned and the kinetic and thermodynamic parameters for the binding were presented. Based on its unique hyperfine shift pattern and the anomalous temperature dependence of the heme methyl resonances, the heme electronic structure was discussed and the orientation of the bound 2mim was estimated. With these data, a comprehensive comparison of imidazole (Him), 4-methylimidazole (4mim) and 2mim bound cyt c complexes was made on the ligand binding affinity and the heme electronic structure. Different properties in these ligand-cyt c complexes provide a useful lesson for the study of protein-small molecular interactions.en_US
dc.languageengen_US
dc.relation.ispartofJournal of the Chemical Society, Dalton Transactionsen_US
dc.title1H NMR study of 2-methylimidazole binding to cytochrome c: A comprehensive investigation of the role of the methyl substituent on the ligand binding affinity and heme electronic structure in imidazole-cytochrome c complexesen_US
dc.typeArticleen_US
dc.identifier.emailQian, C:cmqian@hku.hken_US
dc.identifier.authorityQian, C=rp01371en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-0034743190en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034743190&selection=ref&src=s&origin=recordpageen_US
dc.identifier.issue12en_US
dc.identifier.spage1841en_US
dc.identifier.epage1845en_US
dc.relation.erratumeid:eid_2-s2.0-0035822828-
dc.identifier.scopusauthoridYao, Y=55202633100en_US
dc.identifier.scopusauthoridQian, C=7202311105en_US
dc.identifier.scopusauthoridWu, Y=7406899424en_US
dc.identifier.scopusauthoridHu, J=36077541900en_US
dc.identifier.scopusauthoridTang, W=7403430524en_US

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