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Plant and Cell Physiology, 1985, Vol. 26, No. 5 961-965
© 1985

Short Communication

Inhibition of an aa3-Type Two-Subunit Cytochrome c Oxidase from Nitrobacter agilis by N,N'-Dicyclohexylcarbodiimide

Yoshihiro Fukumori and Tateo Yamanaka

Department of Chemistry, Faculty of Science, Tokyo Institute of Technology O-okayama, Meguro-ku, Tokyo 152, Japan

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.

(Received February 23, 1985; Accepted April 23, 1985)
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