Study of redox potential in cytochrome c covalently bound to terminal oxidase of alkaliphilic Bacillus pseudofirmus FTU
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Spectroelectrochemistry was used to determine the midpoint redox potentials of heme cofactors of the caa 3-type cytochrome oxidase from the alkaliphilic bacterium Bacillus pseudofirmus FTU. The apparent midpoint potentials (E m app ) for the most prominent transitions of hemes a and a 3 (+193 and +334 mV, respectively) were found to be similar to the values reported for other enzymes with high homology to the caa 3-type oxidase. In contrast, the midpoint potential of the covalently bound cytochrome c (+89 mV) was 150–170 mV lower than in cytochromes c, either low molecular weight or covalently bound to the caa 3 complex in all known aerobic neutralophilic and thermo-neutralophilic bacteria. Such an unusually low redox potential of the covalently bound cytochrome c of the caa 3-type oxidase of alkaliphilic bacteria, together with high redox potentials of hemes a and a 3, ensures more than twice higher difference in redox potentials inside the respiratory complex compared to the homologous mitochondrial enzyme. The energy released during this redox transition might be stored in the transmembrane H+ gradient even under low Δp in the alkaline environment of the bacteria at the expense of a significant increase in ΔG of the coupled redox reaction.
Key wordsBacillus pseudofirmus alkaliphile cytochrome c caa3 cytochrome oxidase redox potential
proton motive force
free energy of the reaction
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