By Dunitz J.D.
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Since these two C-5'hydrogens of adenosylcobalamin are not stereochemically equivalent, this observation suggests that during the reductase reaction these two hydrogens become stereochemically equivalent. In contrast to the other adenosylcobalamin-dependent reactions tritium from [5'-alibi adenosylcobalamin is not transferred to the product but only to the solvent. This is a consequence of the fact that in the reductase reaction hydrogen is transferred from a thiol, via adenosylcobalamin to the nucleotide.
For all the systems NADPH is the ultimate reductant, the hydrogen is transferred by thioredoxin reductase to thioredoxin, which in turn is oxidized by ribonucleotide reductase with the concomitant production of a 2'-deoxyribonucleotide. In these systems the thioredoxin-thioredoxin reductase reducing system can be replaced by dithiols such as dihydrolipoate or dithiothreitol. A. The Stereochemistry of the Reduction Initial studies with the enzyme systems from E. coli (84) and from L. leichmannii (85, 86) demonstrated that both reductases catalyze the transfer of hydrogen from water, via the hydrogens of the dithiol, to the deoxyribonucleotide.
N. Sando reductase. T4 thioredoxin does not contain tryptophan and the amino acid sequence around the disulphide bridge is completely different from that of the thioredoxins from E. coli, yeast, Novikoff hepatoma, calf liver and rat liver (44). Presumably these thioredoxins are able to interact with E. coli ribonucleotide reductase because their active sites are very similar or identical, as is the case for the thioredoxins of E. coli and yeast. B. Thioredoxin Reductase Thioredoxin reductase catalyzes the reduction of the oxidized form of thioredoxin by NADPH (36).
Biochemistry. by Dunitz J.D.