Nonenzymatic Model Reaction for the Coenzyme B₁₂‐Catalyzed Rearrangement of Methylmalonyl‐CoA into Succinyl‐CoA

Abstract

Compound (2) was first prepared by Fitjer and Conia by a ten-step synthesis, starting from methyl cyclopropyl ketone, and isolated pure by gasThe hydrocarbon is now more readily accessible by our new synthetic pathway: 3-bromopropyltriphenylphosphonium bromide (3lc3] is reacted with cyclopropanecarbaldehyde (4)[41 in dimethyl sulfoxide (DMSO) in the presence of two equivalents of potassium tert-butoxide to give cyclopropylmethylenecyclopropane (5)r51. Compound ( 5 ) can be brominated in pentane at -17°C in the presence of pyridine

Energetic and Stereochemical Effects of the Protein Environment on Substrate: A Theoretical Study of Methylmalonyl-CoA Mutase

“…Several pathways have been proposed for the mechanism of the 1,2-rearrangement of (2 R )- MMCoA to SuccCoA , , including carbanionic and organo-cobalt species. However, the formation of a cobalt-bound substrate complex seems very unlikely from the arrangement found in crystal structures, and from numerous experiments with model reactions − or in enzyme, − a mechanism involving radicals seems natural.…”

Crystal structure and photolysis spin-trapping EPR investigations of aqua(2-methoxycarbonylethyl)cobaloxime and its β-cyclodextrin inclusion complex †

“…12,13 Among them, the crystal structure of [Co-(n-C 3 H 7 )(HD) 2 (H 2 O)]-α-CD has been reported. 13 Since alkoxycarbonylcobaloximes are often used to model coenzyme B 12 catalysed rearrangement, 14 we wanted to prepare alkoxycarbonylcobaloxime-CD inclusion complexes for structural and photolysis investigation. Here we report a new structure of an aqua(2-methoxycarbonylethyl)cobaloxime-β-CD inclusion complex.…”