Membrane-Bound Redox Enzyme Cytochrome -I Promotes Carbon Monoxide-Resistant Growth and Respiration.

The terminal oxidases of bacterial aerobic respiratory chains are redox-active electrogenic enzymes that catalyze the four-electron reduction of O to 2HO taking out electrons from quinol or cytochrome . Living bacteria often deal with carbon monoxide (CO) which can act as both a signaling molecule and a poison. Bacterial terminal oxidases contain hemes; therefore, they are potential targets for CO. However, our knowledge of this issue is limited and contradictory. Here, we investigated the effect of CO on the cell growth and aerobic respiration of three different mutants, each expressing only one terminal quinol oxidase: cytochrome -I, cytochrome -II, or cytochrome . We found that following the addition of CO to -I-only cells, a minimal effect on growth was observed, whereas the growth of both -II-only and -only strains was severely impaired. Consistently, the degree of resistance of aerobic respiration of -I-only cells to CO is high, as opposed to high CO sensitivity displayed by -II-only and -only cells consuming O. Such a difference between the oxidases in sensitivity to CO was also observed with isolated membranes of the mutants. Accordingly, O consumption of wild-type cells showed relatively low CO sensitivity under conditions favoring the expression of a -type oxidase.