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Article: Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c

TitleSolution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date2001
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB
Citation
European Journal Of Biochemistry, 2001, v. 268 n. 6, p. 1620-1630 How to Cite?
AbstractUsing 1617 meaningful NOEs with 188 pseudocontact shifts, a family of 35 conformers of oxidized bovine microsomal cytochrome b5 mutant (E44/48/56A/D60A) has been obtained and is characterized by good resolution (rmsd to the mean structure are 0.047 ± 0.007 nm and 0.095 ± 0.008 nm for backbone and heavy atoms, respectively). The solution structure of the mutant, when compared with the X-ray structure of wild-type cytochrome b5, has no significant changes in the whole folding and secondary structure. The binding between cytochrome b5 and cytochrome c shows that the association constant of the mutant-cytochrome c complex is much lower than the one for wild-type complex (2.2 × 104 M-1 vs. 5.1 × 103 M-1). The result suggests the four acidic residues have substantial effects on the formation of the complex between cytochrome b5 and cytochrome c, and therefore it is concluded reasonably that the electrostatic interaction plays an important role in maintaining the stability and specificity of the complex formed. The competition between the ferricytochrome b5 mutant and [Cr(oxalate)3]3- for ferricytochrome c shows that site III of cytochrome c, which is a strong binding site to wild-type cytochrome b5, still binds to the mutant with relatively weaker strength. Our results indicate that certain bonding geometries do occur in the interaction between the present mutant and cytochrome c and these geometries, which should be quite different from the ones of the Salemme and Northrup models.
Persistent Identifierhttp://hdl.handle.net/10722/91173
ISSN
2006 Impact Factor: 3.579
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWu, Yen_HK
dc.contributor.authorWang, Yen_HK
dc.contributor.authorQian, Cen_HK
dc.contributor.authorLu, Jen_HK
dc.contributor.authorLi, Een_HK
dc.contributor.authorWang, Wen_HK
dc.contributor.authorLu, Jen_HK
dc.contributor.authorXie, Yen_HK
dc.contributor.authorWang, Jen_HK
dc.contributor.authorZhu, Den_HK
dc.contributor.authorHuang, Zen_HK
dc.contributor.authorTang, Wen_HK
dc.date.accessioned2010-09-17T10:14:11Z-
dc.date.available2010-09-17T10:14:11Z-
dc.date.issued2001en_HK
dc.identifier.citationEuropean Journal Of Biochemistry, 2001, v. 268 n. 6, p. 1620-1630en_HK
dc.identifier.issn0014-2956en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91173-
dc.description.abstractUsing 1617 meaningful NOEs with 188 pseudocontact shifts, a family of 35 conformers of oxidized bovine microsomal cytochrome b5 mutant (E44/48/56A/D60A) has been obtained and is characterized by good resolution (rmsd to the mean structure are 0.047 ± 0.007 nm and 0.095 ± 0.008 nm for backbone and heavy atoms, respectively). The solution structure of the mutant, when compared with the X-ray structure of wild-type cytochrome b5, has no significant changes in the whole folding and secondary structure. The binding between cytochrome b5 and cytochrome c shows that the association constant of the mutant-cytochrome c complex is much lower than the one for wild-type complex (2.2 × 104 M-1 vs. 5.1 × 103 M-1). The result suggests the four acidic residues have substantial effects on the formation of the complex between cytochrome b5 and cytochrome c, and therefore it is concluded reasonably that the electrostatic interaction plays an important role in maintaining the stability and specificity of the complex formed. The competition between the ferricytochrome b5 mutant and [Cr(oxalate)3]3- for ferricytochrome c shows that site III of cytochrome c, which is a strong binding site to wild-type cytochrome b5, still binds to the mutant with relatively weaker strength. Our results indicate that certain bonding geometries do occur in the interaction between the present mutant and cytochrome c and these geometries, which should be quite different from the ones of the Salemme and Northrup models.en_HK
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJBen_HK
dc.relation.ispartofEuropean Journal of Biochemistryen_HK
dc.subjectChemicals And Cas Registry Numbersen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshCytochrome c Group - metabolismen_HK
dc.subject.meshCytochromes b5 - chemistry - genetics - metabolismen_HK
dc.subject.meshMagneticsen_HK
dc.subject.meshModels, Molecularen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshMutationen_HK
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_HK
dc.subject.meshProtein Conformationen_HK
dc.titleSolution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with 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.doi10.1046/j.1432-1327.2001.02033.xen_HK
dc.identifier.pmid11248680en_HK
dc.identifier.scopuseid_2-s2.0-0034825436en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034825436&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume268en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1620en_HK
dc.identifier.epage1630en_HK
dc.identifier.isiWOS:000167703500014-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWu, Y=7406899424en_HK
dc.identifier.scopusauthoridWang, Y=8513746300en_HK
dc.identifier.scopusauthoridQian, C=7202311105en_HK
dc.identifier.scopusauthoridLu, J=36065866500en_HK
dc.identifier.scopusauthoridLi, E=7201410174en_HK
dc.identifier.scopusauthoridWang, W=7501757664en_HK
dc.identifier.scopusauthoridLu, J=26662977000en_HK
dc.identifier.scopusauthoridXie, Y=7403958906en_HK
dc.identifier.scopusauthoridWang, J=7701336117en_HK
dc.identifier.scopusauthoridZhu, D=7403598906en_HK
dc.identifier.scopusauthoridHuang, Z=7406221847en_HK
dc.identifier.scopusauthoridTang, W=7403430524en_HK

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