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• W2027857789 abstract "Cytochrome c oxidase (C c O) is the terminal enzyme of the respiratory chain and couples energetically the reduction of oxygen to water to proton pumping across the membrane. The results from previous studies showed that proton pumping can be uncoupled from the O 2 -reduction reaction by replacement of one single residue, Asn-139 by Asp (N139D), located ≈30 Å from the catalytic site, in the D-proton pathway. The uncoupling was correlated with an increase in the p K a of an internal proton donor, Glu-286, from ≈9.4 to >11. Here, we show that replacement of the acidic residue, Asp-132 by Asn in the N139D C c O (D132N/N139D double-mutant C c O) results in restoration of the Glu-286 p K a to the original value and recoupling of the proton pump during steady-state turnover. Furthermore, a kinetic investigation of the specific reaction steps in the D132N/N139D double-mutant C c O showed that proton pumping is sustained even if proton uptake from solution, through the D-pathway, is slowed. However, during single-turnover oxidation of the fully reduced C c O the P → F transition, which does not involve electron transfer to the catalytic site, was not coupled to proton pumping. The results provide insights into the mechanism of proton pumping by C c O and the structural elements involved in this process." @default.
• W2027857789 created "2016-06-24" @default.
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• W2027857789 date "2006-01-03" @default.
• W2027857789 modified "2023-09-25" @default.
• W2027857789 title "Controlled uncoupling and recoupling of proton pumping in cytochrome <i>c</i> oxidase" @default.
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• W2027857789 doi "https://doi.org/10.1073/pnas.0507734103" @default.
• W2027857789 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1326165" @default.
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