Biochemical catalysis involving coenzyme B-12: a rational stepwise mechanistic interpretation of vicinal interchange rearrangements.
Open Access
- 1 March 1977
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 74 (3) , 811-815
- https://doi.org/10.1073/pnas.74.3.811
Abstract
A mechanism is proposed for the catalytic action of coenzyme B-12 which is consistent with current knowledge of organometallic reactions and with the experimental data now available from biochemical studies. A key feature of the proposal is an electrocyclic cleavage of the coenzyme that reduces cobalt and also leads to a 1,19-seco-corrin. The seco-corrin serves as a tridentate ligand about Co(I). This arrangement permits the metal to take part in the kinds of organometallic reactions that are ideal for coenzyme B-12 catalysis, including oxidative addition and its reverse, reductive elimination. It is further proposed that the rearrangement steps involve cobaltcarbene complexes.This publication has 6 references indexed in Scilit:
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