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- W2040995863 abstract "Dibucaine acts as a weak protonophore in cytochrome c oxidase proteoliposomes. At low concentrations in the presence of permeant anions, it stimulates turnover and collapses enzyme-generated pH gradients. At higher concentrations, dibucaine inhibits activity of cytochrome c oxidase in proteoliposomes and the isolated enzyme. It also induces a red shift in the resting spectrum, indicating a change at the binuclear centre. This spectroscopic effect is kinetically biphasic. Dibucaine inhibits steady-state oxidase activity, but not the rate of the red shift in the cytochrome a 3 Soret band during turnover. It reacts faster with the partially reduced state than with resting enzyme. The inhibition is kinetically biphasic with a noncompetitive K i ≈ 0.5 mM. Excess dibucaine effects a maximal turnover decline of 80%. At low ionic strength only the total V max is affected; tight binding of cytochrome c and turnover at the tight site are unaffected. Dibucaine may bind to an anionic site in a hydrophobic pocket, modifying electron transfer from cytochrome a and Cu A to cytochrome a 3 - Cu B and the oxidized spectrum of the latter centre. Stimulation of turnover in cytochrome c oxidase in proteoliposomes is due to a separate membrane-dependent proton translocation catalysed by dibucaine in the presence of permeant anions.Key words: dibucaine, cytochrome c oxidase, proteoliposomes, respiratory control, inhibition." @default.
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- W2040995863 date "1993-01-01" @default.
- W2040995863 modified "2023-09-27" @default.
- W2040995863 title "Dibucaine interacts differently with membrane and protein in cytochrome c oxidase systems" @default.
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- W2040995863 doi "https://doi.org/10.1139/o93-003" @default.
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