Abstract
AbstractAlcohol dehydrogenase (E.C. 1.1.1.1, abbreviated ADH) isolated from germinating pea seeds (Pisum arvense L.) is inactivated by iodoacetate. The inactivation rate is decreased by ATP, ADP, AMP, NAD, chloride ions and o‐phenanthroline. The nucleotides studied are bound in the area of the coenzyme binding site, similar to iodoacetate. On the other hand, o‐phenanthroline binds zinc ions in a chelate which is apparently bound in the close vicinity of the coenzyme binding site.
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