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Preparation and characterization of a pentaammineruthenium(III) derivative of horse heart ferricytochrome c

Yocom, Kathryn M. and Shelton, Joan B. and Shelton, J. Roger and Schroeder, Walter A. and Worosila, Greg and Isied, Stephan S. and Bordignon, Emilio and Gray, Harry B. (1982) Preparation and characterization of a pentaammineruthenium(III) derivative of horse heart ferricytochrome c. Proceedings of the National Academy of Sciences of the United States of America, 79 (22). pp. 7052-7055. ISSN 0027-8424. PMCID PMC347273. http://resolver.caltech.edu/CaltechAUTHORS:YOCpnas82

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Abstract

A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium binding site. Spectroscopic measurements show that the integrity of the native structure in the vicinity of the heme c group is maintained in the ruthenium-modified protein. The reduction potentials are: heme c (Fe3+/2+), 0.26 V; Ru(NH3)5(His-33)3+/2+, 0.15 V (vs. normal hydrogen electrode).


Item Type:Article
Related URLs:
URLURL TypeDescription
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC347273/PubMed CentralArticle
Additional Information:© 1982 by the National Academy of Sciences. Contributed by Harry B. Gray, August 23, 1982. Our research on cytochrome c derivatives has been aided greatly by numerous discussions with Dick Dickerson, Walther Ellis, John Hopfield, Bo Malmstrom, Rudy Marcus, Chuck Root, Norman Sutin, Henry Taube, and Henrique Toma. NMR spectra were obtained at the Stanford University NMR Laboratory (supported by National Science Foundation Grant GP23633 and National Institutes of Health Grant RR 00711). Research at California Institute of Technology was supported by National Science Foundation Grant CHE80-24863 (K.M.Y., E.B., and H.B.G.) and by National Institutes of Health Grant HL 02558 (J.B.S., J.R.S., and W.A.S.). Research at Rutgers University was supported by National Institutes of Health Grant GM 26324 (S.S.1.). S.S.I. acknowledges a National Institutes of Health Career Development Award (AM 00734) (1980-1985) and a Camille and Henry Dreyfus Teacher-Scholar Award. This is contribution no. 6706 from the Arthur Amos Noyes Laboratory. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.
Funders:
Funding AgencyGrant Number
NSFGP23633
NIHRR 00711
NSFCHE80-24863
NIHHL02558
NIHGM26324
NIHAM00734
Camille and Henry Dreyfus FoundationUNSPECIFIED
Subject Keywords:ruthenium-histidine binding, modified cytochromes, electrochemistry
Other Numbering System:
Other Numbering System NameOther Numbering System ID
Arthur Amos Noyes Laboratory of Chemical Physics6706
PubMed Central ID:PMC347273
Record Number:CaltechAUTHORS:YOCpnas82
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:YOCpnas82
Alternative URL:http://www.pnas.org/cgi/content/abstract/79/22/7052
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:1010
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:01 Dec 2005
Last Modified:30 May 2017 19:13

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