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The nature of CuA in cytochrome c oxidase

Stevens, Tom H. and Martin, Craig T. and Wang, Hsin and Brudvig, Gary W. and Scholes, Charles P. and Chan, Sunney I. (1982) The nature of CuA in cytochrome c oxidase. Journal of Biological Chemistry, 257 (20). pp. 12106-10113. ISSN 0021-9258. http://resolver.caltech.edu/CaltechAUTHORS:STEjbc82

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Abstract

The isolation and purification of yeast cytochrome c oxidase is described. Characterization of the purified protein indicates that it is spectroscopically identical with cytochrome c oxidase isolated from beef heart. Preparations of isotopically substituted yeast cytochrome c oxidase are obtained incorporating [1,3-15N2]histidine or [beta,beta- 2H2]cysteine. Electron paramagnetic resonance and electron nuclear double resonance spectra of the isotopically substituted proteins identify unambiguously at least 1 cysteine and 1 histidine as ligands to CuA and suggest that substantial spin density is delocalized onto a cysteine sulfur in the oxidized protein to render the site Cu(I)-S.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://www.jbc.org/cgi/content/abstract/257/20/12106PublisherArticle
ORCID:
AuthorORCID
Chan, Sunney I.0000-0002-5348-2723
Additional Information:© 1982 by the American Society for Biochemistry and Molecular Biology. (Received for publication, February 18, 1982) We are grateful to Drs. Hal Beilan and Doug Brown for their technical assistance in the synthesis of labeled cysteine in the early stages of this work. We are indebted to Dr. Savely Goldin for assistance in performing the ENDOR measurements and to Dr. Randall Morse for helpful discussions. This paper is Contribution 6444 from the Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, CA 91125. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. [T.H.S. was the] [r]ecipient of National Research Service Award 5T32GM-07616 from the National Institute of General Medical Sciences. [C.P.S. was the] [r]ecipient of Grant AM-17884 from the National Institute of Arthritis, Metabolism, and Digestive Diseases, United States Public Health Service, Grant RR07122 from the Biomedical Research Support Grant Program, Division of Research Resources, National Institutes of Health, and National Institutes of Health Research Career Development Award 1K04 AM-00274. [S.I.C. was the] [r]ecipient of Grant GM-22432 from the National Institutes of General Medical Sciences and Biomedical Research Support Grant RR07003.
Funders:
Funding AgencyGrant Number
NIH Predoctoral Fellowship5T32GM-07616
NIHAM-17884
NIHRR07122
NIH1K04 AM-00274
NIHGM-22432
NIHRR07003
National Institute of General Medical SciencesUNSPECIFIED
National Institute of Arthritis, Metabolism, and Digestive DiseasesUNSPECIFIED
Other Numbering System:
Other Numbering System NameOther Numbering System ID
Arthur Amos Noyes Laboratory of Chemical Physics6444
Issue or Number:20
Record Number:CaltechAUTHORS:STEjbc82
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:STEjbc82
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:12366
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:13 Nov 2008 21:44
Last Modified:26 Sep 2017 19:54

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