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- W2024943035 abstract "Reaction of ubiquinone in the high‐affinity quinone‐binding site (Q H ) in bo ‐type ubiquinol oxidase from Escherichia coli was revealed by EPR and optical studies. In the Q H site, ubiquinol was shown to be oxidized to ubisemiquinone and to ubiquinone, while no semiquinone signal was detected in the oxidase isolated from mutant cells that cannot synthesize ubiquinone. The Q H site highly stabilized ubisemiquinone radical with a stability constant of 1–4 at pH 8.5 and the stability became lower at the lower pH. Midpoint potential of QH 2 /Q couple was −2 mV at pH 8.5 and showed −60 mV/pH dependence indicative of 2H + /2e − reaction. The E m was more negative than that of low‐spin heme b above pH 7.0. We conclude that the Q H mediates intramolecular electron transfer from ubiquinol in the low‐affinity quinol oxidation site (Q L ) to low‐spin heme b . Unique roles of the quinone‐binding sites in the bacterial ubiquinol oxidase are discussed." @default.
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- W2024943035 title "Stabilization of a semiquinone radical at the high-affinity quinone-binding site (Q<sub>H</sub>) of the<i>Escherichia coli bo</i>-type ubiquinol oxidase" @default.
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- W2024943035 doi "https://doi.org/10.1016/0014-5793(95)01125-x" @default.
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