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Article: Structural analysis of zinc-substituted cytochrome c

TitleStructural analysis of zinc-substituted cytochrome c
Authors
KeywordsSpecies Index: Animalia
Equus Caballus
Issue Date2003
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, 2003, v. 8 n. 4, p. 394-400 How to Cite?
AbstractZinc-substituted cytochrome c has been widely used in studies of protein-protein interactions and photo-induced electron transfer reactions between proteins. However, the coordination geometry of zinc in zincsubstituted cyt c has not yet been determined; two different opinions about the coordination have been reached. Here the solution structures of zinc-substituted cytochrome c that might be five-coordinated and six-coordinated have been refined separately by using 1H NMR spectroscopy, and the zinc coordination geometry was determined just by NOE distance constraints. Structural analysis of the energy-minimized average solution structures of both the pentacoordinated and hexacoordinated geometries indicate that that zinc in zinc-substituted cyt c should be bound to both His18 and Met80, which means that the zinc is six-coordinated. RMSD values of the family of 25 six-coordinated structures from the average structure are 0.66 ± 0.13 Å and 1.09 ± 0.16 Å for the backbone and all heavy atoms, respectively. A statistical analysis of the structure indicates its satisfactory quality. Comparison of the solution structure of the six-coordinated energy-minimized average structure of zinc-substituted cytochrome c with the solution structure of reduced cytochrome c reveals that for the overall folding the secondary structure elements are very close. The availability of the structure provides for a better understanding of the protein-protein complex and for electron transfer processes between Zn cyt c and other metalloproteins.
Persistent Identifierhttp://hdl.handle.net/10722/91179
ISSN
2015 Impact Factor: 2.495
2015 SCImago Journal Rankings: 0.882
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorQian, Cen_HK
dc.contributor.authorYao, Yen_HK
dc.contributor.authorTong, Yen_HK
dc.contributor.authorWang, Jen_HK
dc.contributor.authorTang, Wen_HK
dc.date.accessioned2010-09-17T10:14:17Z-
dc.date.available2010-09-17T10:14:17Z-
dc.date.issued2003en_HK
dc.identifier.citationJournal Of Biological Inorganic Chemistry, 2003, v. 8 n. 4, p. 394-400en_HK
dc.identifier.issn0949-8257en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91179-
dc.description.abstractZinc-substituted cytochrome c has been widely used in studies of protein-protein interactions and photo-induced electron transfer reactions between proteins. However, the coordination geometry of zinc in zincsubstituted cyt c has not yet been determined; two different opinions about the coordination have been reached. Here the solution structures of zinc-substituted cytochrome c that might be five-coordinated and six-coordinated have been refined separately by using 1H NMR spectroscopy, and the zinc coordination geometry was determined just by NOE distance constraints. Structural analysis of the energy-minimized average solution structures of both the pentacoordinated and hexacoordinated geometries indicate that that zinc in zinc-substituted cyt c should be bound to both His18 and Met80, which means that the zinc is six-coordinated. RMSD values of the family of 25 six-coordinated structures from the average structure are 0.66 ± 0.13 Å and 1.09 ± 0.16 Å for the backbone and all heavy atoms, respectively. A statistical analysis of the structure indicates its satisfactory quality. Comparison of the solution structure of the six-coordinated energy-minimized average structure of zinc-substituted cytochrome c with the solution structure of reduced cytochrome c reveals that for the overall folding the secondary structure elements are very close. The availability of the structure provides for a better understanding of the protein-protein complex and for electron transfer processes between Zn cyt c and other metalloproteins.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.subjectSpecies Index: Animaliaen_HK
dc.subjectEquus Caballusen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshCytochromes c - chemistryen_HK
dc.subject.meshHorsesen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshMolecular Structureen_HK
dc.subject.meshZinc - chemistryen_HK
dc.titleStructural analysis of zinc-substituted cytochrome 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.pmid12761660-
dc.identifier.scopuseid_2-s2.0-0038288787en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0038288787&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume8en_HK
dc.identifier.issue4en_HK
dc.identifier.spage394en_HK
dc.identifier.epage400en_HK
dc.identifier.isiWOS:000183036300003-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridYao, Y=55202633100en_HK
dc.identifier.scopusauthoridTong, Y=7202614811en_HK
dc.identifier.scopusauthoridWang, J=7701336117en_HK
dc.identifier.scopusauthoridTang, W=7403430524en_HK

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