Abstract
The stereospecific action of the microbial enzyme 4-hydroxybutyryl-CoA dehydratase on the three prochiral centers of its substrate 4-hydroxybutyryl-CoA can now be described as anti elimination of the 2Re and 3Si hydrogen atoms with retention of configuration during the substitution of the hydroxy group by a hydrogen atom. The results confirm the relationship of the dehydratase to acyl-CoA dehydrogenases and the view that the Fe4S4 cluster acts as a Lewis acid.
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