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Published March 10, 1985 | Published
Journal Article Open

The identification of histidine ligands to cytochrome a in cytochrome c oxidase

Abstract

A histidine auxotroph of Saccharomyces cerevisiae has been used to metabolically incorporate [1,3-15N2] histidine into yeast cytochrome c oxidase. Electron nuclear double resonance (ENDOR) spectroscopy of cytochrome a in the [15N]histidine-substituted enzyme reveals an ENDOR signal which can be assigned to hyperfine coupling of a histidine 15N with the low-spin heme, thereby unambiguously identifying histidine as an axial ligand to this cytochrome. Comparison of this result with similar ENDOR data obtained on two 15N-substituted bisimidazole model compounds, metmyoglobin-[15N]imidazole and bis[15N]imidazole tetraphenyl porphyrin, provides strong evidence for bisimidazole coordination in cytochrome a.

Additional Information

© 1985 American Society of Biological Chemists. Received for publication, August 17, 1984. This paper is Contribution 7078 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. [C.T.M. 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-18884 from the National Institute of Arthritis, Metabolism, and Digestive Diseases, United States Public Health Service and Grant RR07122 from the Biomedical Research Support Grant Program, Division of Research Resources, National Institutes of Health. [S.I.C. was the] [r]ecipient of Grant GM-22432 from the National Institute of General Medical Sciences and Biomedical Research Support Grant RR07003.

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August 22, 2023
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October 17, 2023