Abstract
Abstract When 1,2-propanediol-1-3H is converted to propionaldehyde in the presence of dioldehydrase and 5,6-dimethylbenzimidazolylcobamide 5'-deoxyadenosine, 2 hydrogen atoms per mole of the coenzyme are replaced by tritium. The tritiated coenzyme so obtained transfers tritium to the product when it is added to unlabeled 1,2-propanediol and dioldehydrase. The coenzyme containing tritium at C-5' of the adenosyl moiety was prepared synthetically; when it was added to dioldehydrase and unlabeled 1,2-propanediol, all of the tritium initially present in the coenzyme was found in the propionaldehyde. From these results we concluded that the hydrogen transfer that occurs in the conversion of 1,2-propanediol to propionaldehyde involves two steps: transfer of hydrogen from C-1 to the carbon bonded to the cobalt of the coenzyme and, from this position, to C-2 of the product.
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