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Article: Solution structure of cyanoferricytochrome c: Ligand-controlled conformational flexibility and electronic structure of the heme moiety

TitleSolution structure of cyanoferricytochrome c: Ligand-controlled conformational flexibility and electronic structure of the heme moiety
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2002
PublisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htm
Citation
Journal Of Biological Inorganic Chemistry, 2002, v. 7 n. 4-5, p. 539-547 How to Cite?
AbstractThe solution structure of cyanoferricytochrome c has been determined using NMR spectroscopy. As a result of including additional constraints derived from pseudocontact shifts, a high-resolution NMR structure was obtained with high accuracy. In order to study the conformational transition between the native protein and its ligand adducts, the present structure was compared with the solution structures of the wild-type cytochrome c and the imidazole-cytochrome c complex. Like the solution structure of imidazole-cytochrome c, the heme crevice is widened by the swinging out of residues 77-85 and a noticeable shift of the 50s helix. However, unlike imidazole, cyanide exerts less significant perturbation on the conformation of the heme cavity, which is revealed by a more compact residue package in the distal pocket. Furthermore, comparison of the solution structure of CN-iso-1Met80Ala cytochrome c with the structure of cyanoferricytochrome c indicated that the binding of cyanide has a different impact on the distal cavity conformation in the two proteins. In addition, the magnetic properties of the present system are discussed and a comprehensive study of the electronic structure of ligand-cytochrome c complexes and the native protein is also described.
Persistent Identifierhttp://hdl.handle.net/10722/91175
ISSN
2015 Impact Factor: 2.495
2015 SCImago Journal Rankings: 0.882
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYao, Yen_HK
dc.contributor.authorQian, Cen_HK
dc.contributor.authorYe, Ken_HK
dc.contributor.authorWang, Jen_HK
dc.contributor.authorBai, Zen_HK
dc.contributor.authorTang, Wen_HK
dc.date.accessioned2010-09-17T10:14:13Z-
dc.date.available2010-09-17T10:14:13Z-
dc.date.issued2002en_HK
dc.identifier.citationJournal Of Biological Inorganic Chemistry, 2002, v. 7 n. 4-5, p. 539-547en_HK
dc.identifier.issn0949-8257en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91175-
dc.description.abstractThe solution structure of cyanoferricytochrome c has been determined using NMR spectroscopy. As a result of including additional constraints derived from pseudocontact shifts, a high-resolution NMR structure was obtained with high accuracy. In order to study the conformational transition between the native protein and its ligand adducts, the present structure was compared with the solution structures of the wild-type cytochrome c and the imidazole-cytochrome c complex. Like the solution structure of imidazole-cytochrome c, the heme crevice is widened by the swinging out of residues 77-85 and a noticeable shift of the 50s helix. However, unlike imidazole, cyanide exerts less significant perturbation on the conformation of the heme cavity, which is revealed by a more compact residue package in the distal pocket. Furthermore, comparison of the solution structure of CN-iso-1Met80Ala cytochrome c with the structure of cyanoferricytochrome c indicated that the binding of cyanide has a different impact on the distal cavity conformation in the two proteins. In addition, the magnetic properties of the present system are discussed and a comprehensive study of the electronic structure of ligand-cytochrome c complexes and the native protein is also described.en_HK
dc.languageengen_HK
dc.publisherSpringer Verlag. The Journal's web site is located at http://link.springer.de/link/service/journals/00775/index.htmen_HK
dc.relation.ispartofJournal of Biological Inorganic Chemistryen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshCytochrome c Group - chemistry - metabolismen_HK
dc.subject.meshCytochromes cen_HK
dc.subject.meshElectronsen_HK
dc.subject.meshHeme - chemistryen_HK
dc.subject.meshLigandsen_HK
dc.subject.meshMagnetic Resonance Spectroscopyen_HK
dc.subject.meshMagneticsen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshProtein Conformationen_HK
dc.subject.meshSolutionsen_HK
dc.titleSolution structure of cyanoferricytochrome c: Ligand-controlled conformational flexibility and electronic structure of the heme moietyen_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.doi10.1007/s00775-001-0334-yen_HK
dc.identifier.pmid11941512-
dc.identifier.scopuseid_2-s2.0-0036941810en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036941810&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume7en_HK
dc.identifier.issue4-5en_HK
dc.identifier.spage539en_HK
dc.identifier.epage547en_HK
dc.identifier.isiWOS:000174957800020-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridYao, Y=55202633100en_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridYe, K=7102173876en_HK
dc.identifier.scopusauthoridWang, J=7701336117en_HK
dc.identifier.scopusauthoridBai, Z=36985245400en_HK
dc.identifier.scopusauthoridTang, W=7403430524en_HK

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