Abstract
Vitamin B12-dependent enzymes catalyze various methyl transfer reactions and isomerizations accompanied by the initial 1, 2-shift rearrangement. Adenosylcobalamin, which involves both metal-coordinate and organometallic bonds in the same molecule, acts as a true catalyst in the latter reactions. Coenzyme reaction machanisms have been extensively investigated particularly in connection With methylmalonyl-CoA mutase and diol dehydrase, and homolytic cleavage of the Co-C bond as well as its heterolytic cleavage to yield a carbanion intermediate has been postulated. Since cob (I) alamin and its model compounds in Co (I) state act as supernucleophiles, various reactions as catalyzed by these complexes have been examined. For the establishment of effective B12 holoenzyme models, synthetic lipids which form stable single-walled bilayer aggregates in aqueous media are plausibly adopted as apoenzyme models. Novel organometallic chemistry is hopefully developed in the light of biomimetic notions.
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