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Binuclear centre structure of terminal protonmotive oxidases Brown S; Moody AJ; Mitchell R; Rich PRFEBS Lett 1993[Feb]; 316 (3): 216-23The recent proliferation of data obtained from mutant forms of cytochrome oxidase and analogous enzymes has necessitated a re-examination of existing structural models. A new model is proposed, consistent with these data, which brings several protonatable residues (Y244, D298, D300, T309, T316, K319, T326) into the vicinity of the binuclear centre, suggestive of a proton-transferring function. In addition, we also consider those residues which may participate in electron transport between CuA and haem a. We suggest several potential lines of investigation.|Amino Acid Sequence[MESH]|Animals[MESH]|Bacterial Proteins/chemistry[MESH]|Biophysical Phenomena[MESH]|Biophysics[MESH]|Catalysis[MESH]|Cattle[MESH]|Cytochrome b Group/chemistry[MESH]|Electron Transport[MESH]|Electron Transport Complex IV/*chemistry/metabolism[MESH]|Fungal Proteins/chemistry[MESH]|Heme/chemistry[MESH]|Ion Channels[MESH]|Molecular Sequence Data[MESH]|Oxidation-Reduction[MESH]|Protein Conformation[MESH]|Protein Structure, Tertiary[MESH]|Protons[MESH]|Sequence Alignment[MESH] |
