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Article: NMR study of the conformational transition of cytochrome c upon the displacement of Met80 by exogenous ligand: Structural and magnetic characterization of azidoferricytochrome c

TitleNMR study of the conformational transition of cytochrome c upon the displacement of Met80 by exogenous ligand: Structural and magnetic characterization of azidoferricytochrome c
Authors
KeywordsSpecies Index: Equus Caballus
Issue Date2003
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/biophyschem
Citation
Biophysical Chemistry, 2003, v. 103 n. 1, p. 13-23 How to Cite?
AbstractAs the exogenous ligand-cytochrome c complexes were purported to represent models for the unfolding intermediate of cytochrome c, NMR spectroscopy has been utilized to study the azide adduct of horse heart cytochrome c. The structure of azidoferricytochrome c was modeled by restrained energy minimization using paramagenetic pseudocontact shifts as constraints. The bound azide moiety was found to be tilted approximately 15° from the heme normal. The displacement of Met80 by the exogenous azide molecule causes large structural rearrangement in the distal cavity. Furthermore, the conformation transition associated with the swing out of the loop containing Met80 and the shift of the 50s-helix increases the solvent accessibility of the heme group. To elucidate the heme electronic structure of the complex, the paramagnetic 13C shifts were analyzed in terms of a model based on the π molecular orbitals of the heme under perturbed D 4 symmetry. It turned out that the His-Fe bonding provides the protein constraint that orients the in-plane anisotropy in the complex. The electronic properties are in accordance with the calculated magnetic susceptibility anisotropy and the structural information. © 2002 Elsevier Science B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91183
ISSN
2015 Impact Factor: 2.363
2015 SCImago Journal Rankings: 0.929
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYao, Yen_HK
dc.contributor.authorWu, Yen_HK
dc.contributor.authorQian, Cen_HK
dc.contributor.authorYe, Ken_HK
dc.contributor.authorWang, Jen_HK
dc.contributor.authorTang, Wen_HK
dc.date.accessioned2010-09-17T10:14:22Z-
dc.date.available2010-09-17T10:14:22Z-
dc.date.issued2003en_HK
dc.identifier.citationBiophysical Chemistry, 2003, v. 103 n. 1, p. 13-23en_HK
dc.identifier.issn0301-4622en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91183-
dc.description.abstractAs the exogenous ligand-cytochrome c complexes were purported to represent models for the unfolding intermediate of cytochrome c, NMR spectroscopy has been utilized to study the azide adduct of horse heart cytochrome c. The structure of azidoferricytochrome c was modeled by restrained energy minimization using paramagenetic pseudocontact shifts as constraints. The bound azide moiety was found to be tilted approximately 15° from the heme normal. The displacement of Met80 by the exogenous azide molecule causes large structural rearrangement in the distal cavity. Furthermore, the conformation transition associated with the swing out of the loop containing Met80 and the shift of the 50s-helix increases the solvent accessibility of the heme group. To elucidate the heme electronic structure of the complex, the paramagnetic 13C shifts were analyzed in terms of a model based on the π molecular orbitals of the heme under perturbed D 4 symmetry. It turned out that the His-Fe bonding provides the protein constraint that orients the in-plane anisotropy in the complex. The electronic properties are in accordance with the calculated magnetic susceptibility anisotropy and the structural information. © 2002 Elsevier Science B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/biophyschemen_HK
dc.relation.ispartofBiophysical Chemistryen_HK
dc.subjectSpecies Index: Equus Caballusen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshAzides - chemistryen_HK
dc.subject.meshCytochrome c Group - chemistry - metabolismen_HK
dc.subject.meshHeme - chemistryen_HK
dc.subject.meshHorsesen_HK
dc.subject.meshLigandsen_HK
dc.subject.meshMagnetic Resonance Spectroscopyen_HK
dc.subject.meshMethionine - chemistryen_HK
dc.subject.meshModels, Chemicalen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMyocardium - metabolismen_HK
dc.subject.meshProtein Foldingen_HK
dc.subject.meshProtein Structure, Secondaryen_HK
dc.titleNMR study of the conformational transition of cytochrome c upon the displacement of Met80 by exogenous ligand: Structural and magnetic characterization of azidoferricytochrome cen_HK
dc.typeArticleen_HK
dc.identifier.emailQian, C:cmqian@hku.hken_HK
dc.identifier.authorityQian, C=rp01371en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0301-4622(02)00141-2en_HK
dc.identifier.pmid12504251-
dc.identifier.scopuseid_2-s2.0-0037425459en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037425459&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume103en_HK
dc.identifier.issue1en_HK
dc.identifier.spage13en_HK
dc.identifier.epage23en_HK
dc.identifier.isiWOS:000180510500002-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridYao, Y=55202633100en_HK
dc.identifier.scopusauthoridWu, Y=7406899424en_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridYe, K=7102173876en_HK
dc.identifier.scopusauthoridWang, J=7701336117en_HK
dc.identifier.scopusauthoridTang, W=7403430524en_HK

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