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• W2344279333 abstract "Although how an enzyme binds its substrate and rate-limiting transition state is well-studied, how it binds a flexible redox-active coenzyme, which may adopt different native solution conformations when oxidized/reduced, remains unclear. Using the coenzyme nicotinamide adenine dinucleotide (NAD) as an example, we show that redox enzymes bind oxidized NAD+ and reduced NADH in similar conformations that are between folded NAD+ and extended NADH solution conformations. By preorganizing the coenzyme-binding site to bind such an “intermediate” conformation, a redox enzyme can efficiently bind oxidized and reduced NAD, whereas having to substantially reorganize the binding site to accommodate the NAD product might impede catalysis." @default.
• W2344279333 created "2016-06-24" @default.
• W2344279333 creator A5010018908 @default.
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• W2344279333 date "2016-05-02" @default.
• W2344279333 modified "2023-09-25" @default.
• W2344279333 title "Efficient Binding of Flexible and Redox-Active Coenzymes by Oxidoreductases" @default.
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• W2344279333 doi "https://doi.org/10.1021/acscatal.6b00743" @default.
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