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COMPUTATIONAL MODELLING OF COBALAMINDEPENDENT ENZYMATIC REACTIONS: INITIAL STEP OF B12 CATALYSIS IN ADENOSYLCOBALAMIN-DEPENDENT MUTASES AND COB(II)ALAMIN/COB(I)ALAMIN REDOX PROCESS IN METHYL TRANSFERASES Manoj Kumar April 6 , 2012 The role of the active site tyrosine residue in the Co-C5' bond activation in the context of adenosylcobalamin-dependent mutases has been computationally investigated. The density functional, complete active space self-consistent field and quantum mechanics/molecular mechanics calculations have predicted that the deprotonated tyrosine can serve as a redox center potentially causing the one-electron reduction of B12 cofactor. As a result, the reduced form of adenosylcobalamin has been suggested to participate in B12 catalysis and an alternate mechanism for explaining the origin of catalysis in adenosylcobalamindependent mutases has been proposed. The implications of the involvement of the reduced B12 cofactor in the initial step of B12 catalysis that involve Co-C5'

Computational modelling of cobalamin-dependent enzymatic reactions : activation of Co-C bond in adenosylcobalamin-dependent mutases and cob(II)alamin/cob(I)alamin redox process in methyltransferases.