Abstract

The electron transfer activity of an aa3-type two-subunit cytochrome c oxidase of Nitrobacter agilis was inhibited by DCCD. Although the activity of the purified cytochrome c oxidase dissolved in 1% Triton X- 100 was not affected by DCCD even at a ratio of 1,000 mol DCCD per mol cytochrome aa3, the activity of the enzyme dissolved in 0.02% Tween 20 or 0.02% Triton X-100 was inhibited by 60% or more at a ratio of 1,000 mol DCCD per mol cytochrome aa3. The results of SDS polyacrylamide gel electrophoresis of the enzyme incubated with DCCD suggested that subunit II might be a binding site for DCCD.

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