Understanding the mechanism of B-12-dependent methylmalonyl-CoA mutase: Partial proton transfer in action (CROSBI ID 263847)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Smith, David M. ; Golding, Bernard T. ; Radom, Leo
engleski
Understanding the mechanism of B-12-dependent methylmalonyl-CoA mutase: Partial proton transfer in action
Ab initio molecular orbital theory is used to investigate several possible mechanisms involving free radical intermediates for the coenzyme-B-12-dependent rearrangement catalyzed by methylmalonyl-CoA mutase. Our calculations suggest that an intermolecular pathway in which transient fragmentation of the substrate-derived radical is followed by recombination of the fragments ("fragmentation-recombination") is unlikely, but not out of the question, An alternative intramolecular pathway ("addition-elimination") is found to be energetically more favorable. Protonation of the species involved in this latter pathway is found to further reduce the barrier for rearrangement, Examination of the middle ground between the protonated and unprotonated intramolecular mechanisms reveals a continuous spectrum of behavior and demonstrates the potential importance of partial proton transfer. Support for this proposal is obtained from the X-ray crystal structure of the protein. The stereochemistry of the rearrangement has also been examined and bads to a new proposal consistent with experiment.
ELECTRON-PARAMAGNETIC-RESONANCE ; CARBON SKELETON REARRANGEMENT ; BARRIER HYDROGEN-BOND ; COENZYME-A MUTASE ; THEORETICAL PROCEDURES ; ENZYMATIC CATALYSIS ; TRANSITION-STATES ; RADICAL REACTION ; MODEL ; ENZYMES
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Podaci o izdanju
121 (40)
1999.
9388-9399
objavljeno
0002-7863
10.1021/ja991649a