Cytochrome bo from E. coli does not exhibit the same proton transfer characteristics as the bovine cytochrome c oxidase during oxygen reduction.
The reaction where fully reduced cytochrome bo from E. coli partially reduces dioxygen has been characterized with respect to the kinetics of the associated proton uptake, and with respect to the pH- and D2O-sensitivity of the electron transfer reactions. A monophasic proton uptake with a rate constant of about 8 x 10(3) s-1 and a stoichiometry of 0.8 H+/bo were recorded, using the indicator dye, Cresol red, at pH 8.2. The electron transfer reactions were independent of pH in the range 6.0-9.5 and were not affected by exchanging H2O to D2O as solvent. Comparison of these results with those obtained in an earlier investigation of the bovine cytochrome c oxidase [(1992) Biochemistry 31, 11853-11859], indicates differences between the two oxidases with respect to the role of protons in oxygen reduction and/or the mechanism of proton uptake from the medium.
Department of Biochemistry and Biophysics, Chalmers University of Technology, Göteborg, Sweden.
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Hallén
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Svensson
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Nilsson
D000818:Animals; D002417:Cattle; D003573:Cytochrome b Group; D003580:Cytochromes / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D011522:Protons; D012997:Solvents
D003573:Cytochrome b Group; D003580:Cytochromes; D029968:Escherichia coli Proteins; D011522:Protons; D012997:Solvents; C017168:cytochrome bo, E coli; D003576:Electron Transport Complex IV; D010100:Oxygen