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• W2078771309 startingPage "565" @default.
• W2078771309 abstract "Two different pathways through which protons access cytochrome c oxidase operate during oxygen reduction from the mitochondrial matrix, or the bacterial cytoplasm. Here, we use electrocatalytic current measurements to follow oxygen reduction coupled to proton uptake in cytochrome c oxidase isolated from Paracoccus denitrificans. Wild type enzyme and site-specific variants with defects in both proton uptake pathways (K354M, D124N and K354M/D124N) were immobilized on gold nanoparticles, and oxygen reduction was probed electrochemically in the presence of varying concentrations of Zn(2+) ions, which are known to inhibit both the entry and the exit proton pathways in the enzyme. Our data suggest that under these conditions substrate protons gain access to the oxygen reduction site via the exit pathway." @default.
• W2078771309 created "2016-06-24" @default.
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• W2078771309 date "2015-01-27" @default.
• W2078771309 modified "2023-10-04" @default.
• W2078771309 title "Electrochemistry suggests proton access from the exit site to the binuclear center inParacoccus denitrificanscytochromecoxidase pathway variants" @default.
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• W2078771309 doi "https://doi.org/10.1016/j.febslet.2015.01.014" @default.
• W2078771309 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25637325" @default.
• W2078771309 hasPublicationYear "2015" @default.
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