Reference: Martin CT, et al. (1985) The identification of histidine ligands to cytochrome a in cytochrome c oxidase. J Biol Chem 260(5):2857-61

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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.

Reference Type
Journal Article | Research Support, U.S. Gov't, P.H.S. | Comparative Study
Authors
Martin CT, Scholes CP, Chan SI
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