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Abstract
By simultaneous analysis of the on-time distribution and autocorrelation function of a single working cholesterol oxidase enzyme, a diffusional model reveals the coupling of conformation change with enzyme action. Active-site oxidation induces a conformational change that opens the path for substrate entry. Its binding, in turn, induces the reverse protein relaxation process, which tightens the active site, thereby reducing the rate of product release.
Published Version
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