Published February 10, 1981
| Published
Journal Article
Open
Histidine is the axial ligand to cytochrome alpha 3 in cytochrome c oxidase
- Creators
- Stevens, Tom H.
-
Chan, Sunney I.
Chicago
An error occurred while generating the citation.
Abstract
The nitric oxide-bound complexes of reduced yeast cytochrome c oxidase incorporated with [1,3-15N2]histidine have been investigated by EPR spectroscopy. The results of this study have allowed the unambiguous identification of histidine as the endogenous axial ligand to cytochrome alpha 3.
Additional Information
Copyright © 1981 by the American Society for Biochemistry and Molecular Biology. (Received for publication, October 30, 1980) This work was supported by Grant GM-22432 from the National Institute of General Medical Sciences, United States Public Health Service, by BRSG Grant RR07003 awarded by the Biomedical Research Support Grant Program, Division of Research Resources, National Institutes of Health, and by National Research Service Award 1T32 GM-07616 from the National Institute of General Medical Sciences. Contribution No. 6334 from the Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, Calif. 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.Attached Files
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Additional details
- Eprint ID
- 11604
- Resolver ID
- CaltechAUTHORS:STEjbc81
- NIH
- GM-22432
- NIH
- BRSG RR07003
- NIH Predoctoral Fellowship
- 1T32 GM-0761
- National Institute of General Medical Sciences
- Created
-
2008-09-09Created from EPrint's datestamp field
- Updated
-
2019-10-03Created from EPrint's last_modified field
- Other Numbering System Name
- Arthur Amos Noyes Laboratory of Chemical Physics
- Other Numbering System Identifier
- 6334