Dr. Lim, Carmay 林小喬 博士



Efficient Binding of Flexible and Redox-Active Coenzymes by Oxidoreductases

ACS Catalysis, Jun 03, 2016

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.

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