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

A. Jongejan; J. A. Jongejan; W. R. Hagen

doi:https://doi.org/10.1002/jcc.1128

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

A. Jongejan, J. A. Jongejan, W. R. Hagen

Research output: Contribution to journal › Article › Academic › peer-review

12 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1732-1749
Number of pages	18
Journal	Journal of Computational Chemistry
Volume	22
Issue number	15
DOIs	https://doi.org/10.1002/jcc.1128
Publication status	Published - 30 Nov 2001

Keywords

Direct hydride transfer
PQQ
Pyrroloquinoline quinone
Quinoprotein alcohol dehydrogenase
Transition state

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https://doi.org/10.1002/jcc.1128

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title = "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.",

keywords = "Direct hydride transfer, PQQ, Pyrroloquinoline quinone, Quinoprotein alcohol dehydrogenase, Transition state",

author = "A. Jongejan and Jongejan, {J. A.} and Hagen, {W. R.}",

year = "2001",

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TY - JOUR

T1 - Direct hydride transfer in the reaction mechanism of quinoprotein alcohol dehydrogenases

T2 - A quantum mechanical investigation

AU - Jongejan, A.

AU - Jongejan, J. A.

AU - Hagen, W. R.

PY - 2001/11/30

Y1 - 2001/11/30

N2 - 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.

AB - 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.

KW - Direct hydride transfer

KW - PQQ

KW - Pyrroloquinoline quinone

KW - Quinoprotein alcohol dehydrogenase

KW - Transition state

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U2 - https://doi.org/10.1002/jcc.1128

DO - https://doi.org/10.1002/jcc.1128

M3 - Article

SN - 0192-8651

VL - 22

SP - 1732

EP - 1749

JO - Journal of Computational Chemistry

JF - Journal of Computational Chemistry

IS - 15

ER -

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

Abstract

Keywords

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