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Article: Effects of Surface Negatively Charged Amino Acid Mutation on Binding between Cytochrome b 5 and Cytochrome c

TitleEffects of Surface Negatively Charged Amino Acid Mutation on Binding between Cytochrome b 5 and Cytochrome c
Authors
KeywordsBinding
Cytochrome B 5
Cytochrome C
Electrostatic Interaction
Mutant
Issue Date2002
PublisherJilin Daxue. The Journal's web site is located at http://www.cjcu.jlu.edu.cn/
Citation
Kao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal Of Chinese Universities, 2002, v. 23 n. 7, p. 1298 How to Cite?
AbstractThe binding between different Cytochrome b 5 mutants and Cytochrome c has been studied by using of NMR method. The result shows that electrostatic effect plays an important role in maintaining the stability and specificity of the complex formed. The differences in association constants demonstrate the electrostatic contributions of Cytochrome b 5 surface negatively charged residues, which are suggested to be involved in the complex formation in the Brownian dynamics simulations and Salemme models, and to have a significant degree of additivity to the stability of Cyt c-Cyt b 5 complex, and the contribution of Glu48 is a little higher than that of Glu44. Moreover, our result suggests that the docking geometry obtained from Brownian dynamics simulations by Northrup et al, which was involved in the participation of Glu48, Glu56, Asp60 and heme propionate of Cytochrome b 5, do occur in the association between Cytochrome b 5 and Cytochrome c. The competition between the ferricytochrome b 5 mutant I (E48, E56/A, D60/A) 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 b 5, still binds to the mutant with relatively weaker strength. Our results indicate that there are other docking domains between Cyt b 5 and Cyt c different from the above mentioned one from Brownian dynamics simulations, at the same time, it also implies that electrostatic interaction on the wild-type Cyt b 5 and Cyt c interface results in flexible association complexes.
Persistent Identifierhttp://hdl.handle.net/10722/147493
ISSN
2015 Impact Factor: 0.791
2015 SCImago Journal Rankings: 0.211
References

 

DC FieldValueLanguage
dc.contributor.authorQian, CMen_US
dc.contributor.authorWang, YHen_US
dc.contributor.authorWang, WHen_US
dc.contributor.authorYao, Yen_US
dc.contributor.authorHu, Jen_US
dc.contributor.authorLu, JXen_US
dc.contributor.authorXie, Yen_US
dc.contributor.authorHuang, ZXen_US
dc.contributor.authorTang, WXen_US
dc.date.accessioned2012-05-29T06:04:06Z-
dc.date.available2012-05-29T06:04:06Z-
dc.date.issued2002en_US
dc.identifier.citationKao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal Of Chinese Universities, 2002, v. 23 n. 7, p. 1298en_US
dc.identifier.issn0251-0790en_US
dc.identifier.urihttp://hdl.handle.net/10722/147493-
dc.description.abstractThe binding between different Cytochrome b 5 mutants and Cytochrome c has been studied by using of NMR method. The result shows that electrostatic effect plays an important role in maintaining the stability and specificity of the complex formed. The differences in association constants demonstrate the electrostatic contributions of Cytochrome b 5 surface negatively charged residues, which are suggested to be involved in the complex formation in the Brownian dynamics simulations and Salemme models, and to have a significant degree of additivity to the stability of Cyt c-Cyt b 5 complex, and the contribution of Glu48 is a little higher than that of Glu44. Moreover, our result suggests that the docking geometry obtained from Brownian dynamics simulations by Northrup et al, which was involved in the participation of Glu48, Glu56, Asp60 and heme propionate of Cytochrome b 5, do occur in the association between Cytochrome b 5 and Cytochrome c. The competition between the ferricytochrome b 5 mutant I (E48, E56/A, D60/A) 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 b 5, still binds to the mutant with relatively weaker strength. Our results indicate that there are other docking domains between Cyt b 5 and Cyt c different from the above mentioned one from Brownian dynamics simulations, at the same time, it also implies that electrostatic interaction on the wild-type Cyt b 5 and Cyt c interface results in flexible association complexes.en_US
dc.languageengen_US
dc.publisherJilin Daxue. The Journal's web site is located at http://www.cjcu.jlu.edu.cn/en_US
dc.relation.ispartofKao Teng Hsueh Hsiao Hua Heush Hsueh Pao/ Chemical Journal of Chinese Universitiesen_US
dc.subjectBindingen_US
dc.subjectCytochrome B 5en_US
dc.subjectCytochrome Cen_US
dc.subjectElectrostatic Interactionen_US
dc.subjectMutanten_US
dc.titleEffects of Surface Negatively Charged Amino Acid Mutation on Binding between Cytochrome b 5 and Cytochrome cen_US
dc.typeArticleen_US
dc.identifier.emailQian, CM:cmqian@hku.hken_US
dc.identifier.authorityQian, CM=rp01371en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-0346707625en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0346707625&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume23en_US
dc.identifier.issue7en_US
dc.identifier.spage1298en_US
dc.publisher.placeChinaen_US
dc.identifier.scopusauthoridQian, CM=7202311105en_US
dc.identifier.scopusauthoridWang, YH=8513746300en_US
dc.identifier.scopusauthoridWang, WH=7501757664en_US
dc.identifier.scopusauthoridYao, Y=55202633100en_US
dc.identifier.scopusauthoridHu, J=36077541900en_US
dc.identifier.scopusauthoridLu, JX=26662977000en_US
dc.identifier.scopusauthoridXie, Y=7403958906en_US
dc.identifier.scopusauthoridHuang, ZX=7406221847en_US
dc.identifier.scopusauthoridTang, WX=7403430524en_US

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