The identification of histidine ligands to cytochrome a in cytochrome c oxidase.
Copyright policy )The identification of histidine ligands to cytochrome a in cytochrome c oxidase.
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.
- Yale University United States
- State University of New York at Potsdam United States
- California Institute of Technology United States
Electron Transport Complex IV, Myocardium, Cytochrome a Group, Electron Spin Resonance Spectroscopy, Animals, Cytochromes, Cattle, Histidine, Saccharomyces cerevisiae
Electron Transport Complex IV, Myocardium, Cytochrome a Group, Electron Spin Resonance Spectroscopy, Animals, Cytochromes, Cattle, Histidine, Saccharomyces cerevisiae
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