Complexes in Biochemistry by J D Dunitz; et al

By J D Dunitz; et al

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3. ~ It \ + I~ Fig. 4. General reaction for the synthesis of alkylcorrinoids 51 J. 1VL Wood and D. G. :Brown It soon became apparent that the biologically active forms of Vitamin B12 contained the unique Co--C-a-bond, and the instability of these covalent compounds to visible light facilitated observations on the occurrence of functional corrinoids in a number of enzymes. Deoxyadenosylcobalamin was found to be the most abundant corrinoid in bacteria (24) and in mammalian liver (25). Methylcobalamin was found in Escherichia coli (26), calf liver and human blood plasma (27), and also in a number of Clostridia (28).

In general, these enzymes as a group involve the replacement of a ligand attached to one carbon atom of the substrate molecule b y a hydrogen atom from an adjacent carbon atom. These reactions have been viewed as internal oxidation-reduction reactions (Fig. 5). Included in this category of reactions are glutamate mutase (31) methylmalonyl CoA mutase (32), dioldehydrase (33), glycerol dehydrase (34), ethanolamine ammonia-lyase (35) und L-fl-lysine isomerase (36). COENZYME Fig. 5. General mechanism for 5"-deoxyadenosylcorrinoid catalyzed hydrogen transfer Ribonucleotide reductase (37) belongs to this group of reactions also, but for this enzyme the hydrogen donor and hydrogen acceptor are different molecules.

22static. This is confirmed by the binding of PtBr4 , PdI4 and Hgls to the same site. PdCI~- and PdBr~- bind in a different site close to histidine 15 and lysine 96. It could well be that these anions react by substitution with the histidine. The [PtC14] 2- is not strongly bound in this protein. We are grateful to Dr. C. C. F. Blake (Oxford) for the above information. In ribonuclease-S [PtC14] 2- binds to the sulphur of methionine (63). In this case however greater interest centres on the use of cis-[PtenC12] which is one of the best anti-tumour agents.

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