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- W1969131292 abstract "A CuB-deficient mutant of the Escherichia coli bo-type ubiquinol oxidase exhibits a very low oxidase activity that is consistent with a decreased dioxygen binding rate. During the turnover, a photolabile reaction intermediate persists for a few hundred milliseconds, due to much slower heme o-to-ligand electron transfer. Thus, the lack of CuB seems to have endowed the mutant enzyme with myoglobin-like properties, thereby stabilizing the CO-bound form, too. Accordingly we conclude that CuB plays a pivotal role in preferential trapping and efficient reduction of dioxygen at the heme-copper binuclear center." @default.
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- W1969131292 date "1995-08-21" @default.
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- W1969131292 title "CuBpromotes both binding and reduction of dioxygen at the heme-copper binuclear center in theEscherichia coli bo-type ubiquinol oxidase" @default.
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- W1969131292 doi "https://doi.org/10.1016/0014-5793(95)00852-z" @default.
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