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Article: Ruthenium-modified proteins. Reactions of cis-[ Ru(NH3)4(OH2)2]2+ and cis-[ Ru(en)2(OH2)2]2+ with azurin, myoglobin and cytochrome c

TitleRuthenium-modified proteins. Reactions of cis-[ Ru(NH3)4(OH2)2]2+ and cis-[ Ru(en)2(OH2)2]2+ with azurin, myoglobin and cytochrome c
Authors
Che, CMMargalit, RHueyJenn, CGray, HB
Issue Date1987
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/ica
Citation
Inorganica Chimica Acta, 1987, v. 135 n. 1, p. 33-35 How to Cite?
DOI: http://dx.doi.org/10.1016/S0020-1693(00)83257-0
AbstractReactions of cis-[Ru(en)2(OH2)2]2+ (or cis-[Ru (NH3)4(OH2)2]2+) with Pseudomonas aeruginosa azurin (Az), horse heart myoglobin (Mbh), and horse heart cytochrome c (cyt c) give Ru-labelled proteins. The ruthenium binding sites in the singly modified derivatives are His-83 (Az), His-81 (Mbh), and His-33 (cyt c). Spectroscopic and electrochemical measurements indicate that the structures of the proteins are not perturbed by the surface-bound ruthenium complexes. The E°f values of the Ru(III)/(II) couple in these Ru-modified proteins fall between -0.07 and -0.13 V vs. NHE. © 1987.
Persistent Identifierhttp://hdl.handle.net/10722/167403
ISSN
0020-1693
2021 Impact Factor: 3.118
2020 SCImago Journal Rankings: 0.437
ISI Accession Number ID
WOS:A1987F650700009

 

DC FieldValueLanguage
dc.contributor.authorChe, CMen_US
dc.contributor.authorMargalit, Ren_US
dc.contributor.authorHueyJenn, Cen_US
dc.contributor.authorGray, HBen_US
dc.date.accessioned2012-10-08T03:06:32Z-
dc.date.available2012-10-08T03:06:32Z-
dc.date.issued1987en_US
dc.identifier.citationInorganica Chimica Acta, 1987, v. 135 n. 1, p. 33-35en_US
dc.identifier.issn0020-1693en_US
dc.identifier.urihttp://hdl.handle.net/10722/167403-
dc.description.abstractReactions of cis-[Ru(en)2(OH2)2]2+ (or cis-[Ru (NH3)4(OH2)2]2+) with Pseudomonas aeruginosa azurin (Az), horse heart myoglobin (Mbh), and horse heart cytochrome c (cyt c) give Ru-labelled proteins. The ruthenium binding sites in the singly modified derivatives are His-83 (Az), His-81 (Mbh), and His-33 (cyt c). Spectroscopic and electrochemical measurements indicate that the structures of the proteins are not perturbed by the surface-bound ruthenium complexes. The E°f values of the Ru(III)/(II) couple in these Ru-modified proteins fall between -0.07 and -0.13 V vs. NHE. © 1987.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/icaen_US
dc.relation.ispartofInorganica Chimica Actaen_US
dc.titleRuthenium-modified proteins. Reactions of cis-[ Ru(NH3)4(OH2)2]2+ and cis-[ Ru(en)2(OH2)2]2+ with azurin, myoglobin and cytochrome cen_US
dc.typeArticleen_US
dc.identifier.emailChe, CM:cmche@hku.hken_US
dc.identifier.authorityChe, CM=rp00670en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0020-1693(00)83257-0-
dc.identifier.scopuseid_2-s2.0-0011761261en_US
dc.identifier.volume135en_US
dc.identifier.issue1en_US
dc.identifier.spage33en_US
dc.identifier.epage35en_US
dc.identifier.isiWOS:A1987F650700009-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridChe, CM=7102442791en_US
dc.identifier.scopusauthoridMargalit, R=7005792437en_US
dc.identifier.scopusauthoridHueyJenn, C=24430453600en_US
dc.identifier.scopusauthoridGray, HB=36047602600en_US
dc.identifier.issnl0020-1693-

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