Dibutylchloromethyl tin chloride (DBCT) inhibits coupled and uncoupled respiration of mitochondria from potato tubers, cauliflower florets and etiolated mung bean hypocotyls with succinate and L-malate but not with external NADH or TMPD/ascorbate as substrates. Using potato and cauliflower mitochondria. DBCT at 200 pmole/mg of protein gives complete inhibition only in KCl-based media and at pH 6.8. DBCT has no effect on the internal pH of mung bean mitochondria, but does cause a decrease in the membrane potential. Electron transport through the alternative oxidase is not inhibited, neither is the ATP-synthase system. DBCT appears to interact with the functionally-distinct pool of ubiquinone associated with the oxidation of succinate and L-malate.
Applying the law of mass action to a system where an inhibitor binds to an enzyme and pursuing the arguments presented by Easson & Stedman (1936) and Straus & Goldstein (1943), the following equations can be derived:
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