The First Step and the Cob(II)alamin Cofactor Inactive Particles Reactivation in the Updated Mechanism of the Methionine Synthase Process by Tudor Spataru

Author:Tudor Spataru
Format: pdf
Tags: The Methionine Synthase process, in principle, can take an unlimited number of turnovers in the presence of the AdoMet substrate. In the absence of this substrate, the Methionine Synthase process lasts only about 2000 turnovers. During 2000 turnovers, the entire amount of methylcob(II)alamin cofactor is converted into inactive cob(II)alamin particles. Nevertheless, the mechanism of the Methionine Synthase process determined previously lacks the presence of the AdoMet substrate. On the other hand, the first step of this mechanism was only mentioned earlier without its analysis. The CASSCF geometry optimization of the inactive cob(II)alamin cofactor particle plus the AdoMet ion substrate and of the methylcob(II)alamin cofactor particle plus homocysteine ion and histidine molecule joint models have been performed. CASSCF calculations show that the AdoMet particle transfers the methyl radical to the biologically inactive cob(II)alamin particle during their interaction, transforming it into the biologically active particle of methylcob(II)alamin. CASSCF geometry optimization of the second model leads to the Co-N bond’s full cleavage. The two processes take place in the absence of the total energy barrier. The fully updated mechanism of the Methionine Synthase process has been drawn., vitamin B12; Methionine Synthase; methylcobalamin cofactor; CASSCF; MCSCF


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