Direct hydride transfer in the reaction mechanism of quinoprotein alcohol dehydrogenases: a quantum mechanical investigation

Abstract
Oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone (PQQ) cofactor of quinoprotein alcohol dehydrogenases has been studied using ab initio quantum mechanical methods. Energies and geometries were calculated at the 6‐31G(d,p) level of theory. Comparison of the results obtained for PQQ and several derivatives with available structural and spectroscopic data served to judge the feasibility of the calculations. The role of calcium in the enzymatic reaction mechanism has been investigated. Transition state searches have been conducted at the semiempirical and STO‐3G(d) level of theory. It is concluded that hydride transfer from the Cα‐position of the substrate alcohol (or aldehyde) directly to the C(5) carbon of PQQ is energetically feasible. © 2001 John Wiley & Sons, Inc. J Comput Chem 22: 1732–1749, 2001

This publication has 71 references indexed in Scilit: