Thermophilic bacilli contain cytochrome caa(3)-type cytochrome c oxidase as the main terminal oxidase in the respiratory chain. A mutant strain, named K-17, Backing cytochrome caa(3) and exhibiting very low N,N,N',N'-tetramethyl-p-phenylene diamine oxidase activity, was isolated by random mutation from Bacillus stearothermophilus K1041 (Sakamoto, J. et al., FEMS Microbiol. Lett., 143, 151-158, 1996). Comparing this mutant with the parent strain K1041, we observed the following differences in energy-yielding properties. (i) K-17 gave an cell yield less than one half of that of the wild type, although the doubling time of K-17 was only a little slower than that of the parent strain. (ii) In cellular respiration, the H+/O ratio of K-17 was 2.9-3.1, while that of the wild type was 6.1-6.5. (iii) A low concentration of cyanide inhibited endogenous respiration of the wild-type cells partly with a concomitant reduction of the H+/O ratio to around 3, while it did not significantly affect the respiration rate and the H+/O ratio of the K-17 cells. (iv) Cytochrome bd-type quinol oxidase seemed to operate in the wild-type cells when a low concentration (below 0.5 mM) of cyanide was added, while this enzyme Is the main terminal oxidase in K-17. The K-17 cells also contained cytochrome b(o/a)(3)-type cytochrome c-551 oxidase. These results demonstrated that the combination of the enzymes involved in the respiratory chain determines the H+/O ratios of the cell and consequently the growth yield of the bacteria.