Biochemical catalysis involving coenzyme B-12: a rational stepwise mechanistic interpretation of vicinal interchange rearrangements. | Zendy

E. J. Corey | Zendy; N. John Cooper | Zendy; M L Green | Zendy

Open Access

Biochemical catalysis involving coenzyme B-12: a rational stepwise mechanistic interpretation of vicinal interchange rearrangements.

Author(s) -

E. J. Corey,

N. John Cooper,

M L Green

Publication year - 1977

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.74.3.811

Subject(s) - corrin , chemistry , cofactor , vicinal , stereochemistry , catalysis , combinatorial chemistry , ligand (biochemistry) , oxidative addition , cobalt , organic chemistry , biochemistry , enzyme , receptor

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.

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