Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols

Sonia S. Machado; Aldo Jongejan; Arie Geerlof; Jaap A. Jongejan; Johannis A. Duine

doi:https://doi.org/10.3109/10242429909040114

Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols

Sonia S. Machado, Aldo Jongejan, Arie Geerlof, Jaap A. Jongejan, Johannis A. Duine

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

2 Citations (Scopus)

Abstract

Quinohaemoprotein alcohol dehydrogenases, QH-ADHs, show appreciable enantioselectivity in the oxidation of certain chiral primary and secondary alcohols. We determined the effect of temperature on the enantiomeric ratio of structurally related enzymes, QH-ADH, Type I, from Comamonas testosteroni and QH-ADH, Type II, from Acetobacter pasteurianus, in the kinetic resolution of racemic 2,2-dimethyl-4-(hydroxymethyl)-1,3-dioxolane (solketal) and 2-butanol, respectively. It appears that entropic contributions to the stabilization of the enantioselectivity-determining transition state play an important role in the enantiopreference. Consequences of these findings for the formulation of models that can be used to summarise the observed enantioselectivities are discussed.

Original language	English
Pages (from-to)	179-207
Number of pages	29
Journal	Biocatalysis and Biotransformation
Volume	17
Issue number	3
DOIs	https://doi.org/10.3109/10242429909040114
Publication status	Published - 1999

Keywords

Acetobacter pasteurianus
Comamonas testosteroni
Enantioselectivity
Enthalpy
Entropy
Oxidation
Quinohaemoprotein alcohol dehydrogenase
Temperature

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Machado, S. S., Jongejan, A., Geerlof, A., Jongejan, J. A., & Duine, J. A. (1999). Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols. Biocatalysis and Biotransformation, 17(3), 179-207. https://doi.org/10.3109/10242429909040114

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abstract = "Quinohaemoprotein alcohol dehydrogenases, QH-ADHs, show appreciable enantioselectivity in the oxidation of certain chiral primary and secondary alcohols. We determined the effect of temperature on the enantiomeric ratio of structurally related enzymes, QH-ADH, Type I, from Comamonas testosteroni and QH-ADH, Type II, from Acetobacter pasteurianus, in the kinetic resolution of racemic 2,2-dimethyl-4-(hydroxymethyl)-1,3-dioxolane (solketal) and 2-butanol, respectively. It appears that entropic contributions to the stabilization of the enantioselectivity-determining transition state play an important role in the enantiopreference. Consequences of these findings for the formulation of models that can be used to summarise the observed enantioselectivities are discussed.",

keywords = "Acetobacter pasteurianus, Comamonas testosteroni, Enantioselectivity, Enthalpy, Entropy, Oxidation, Quinohaemoprotein alcohol dehydrogenase, Temperature",

author = "Machado, {Sonia S.} and Aldo Jongejan and Arie Geerlof and Jongejan, {Jaap A.} and Duine, {Johannis A.}",

note = "Funding Information: We gratefully acknowledge the financial support from the Conselho Nacional de Desenvolvimento Cientifico e Tecnologico/CNPq, Brasil (S.S.M.) and the Organization for the Advancement of Pure Research/ NWO, Foundation for Chemical Research/SON, The Netherlands (A.J.).",

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doi = "https://doi.org/10.3109/10242429909040114",

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Machado, SS, Jongejan, A, Geerlof, A, Jongejan, JA & Duine, JA 1999, 'Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols', Biocatalysis and Biotransformation, vol. 17, no. 3, pp. 179-207. https://doi.org/10.3109/10242429909040114

Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols. / Machado, Sonia S.; Jongejan, Aldo; Geerlof, Arie et al.
In: Biocatalysis and Biotransformation, Vol. 17, No. 3, 1999, p. 179-207.

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

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T1 - Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols

AU - Machado, Sonia S.

AU - Jongejan, Aldo

AU - Geerlof, Arie

AU - Jongejan, Jaap A.

AU - Duine, Johannis A.

N1 - Funding Information: We gratefully acknowledge the financial support from the Conselho Nacional de Desenvolvimento Cientifico e Tecnologico/CNPq, Brasil (S.S.M.) and the Organization for the Advancement of Pure Research/ NWO, Foundation for Chemical Research/SON, The Netherlands (A.J.).

PY - 1999

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N2 - Quinohaemoprotein alcohol dehydrogenases, QH-ADHs, show appreciable enantioselectivity in the oxidation of certain chiral primary and secondary alcohols. We determined the effect of temperature on the enantiomeric ratio of structurally related enzymes, QH-ADH, Type I, from Comamonas testosteroni and QH-ADH, Type II, from Acetobacter pasteurianus, in the kinetic resolution of racemic 2,2-dimethyl-4-(hydroxymethyl)-1,3-dioxolane (solketal) and 2-butanol, respectively. It appears that entropic contributions to the stabilization of the enantioselectivity-determining transition state play an important role in the enantiopreference. Consequences of these findings for the formulation of models that can be used to summarise the observed enantioselectivities are discussed.

AB - Quinohaemoprotein alcohol dehydrogenases, QH-ADHs, show appreciable enantioselectivity in the oxidation of certain chiral primary and secondary alcohols. We determined the effect of temperature on the enantiomeric ratio of structurally related enzymes, QH-ADH, Type I, from Comamonas testosteroni and QH-ADH, Type II, from Acetobacter pasteurianus, in the kinetic resolution of racemic 2,2-dimethyl-4-(hydroxymethyl)-1,3-dioxolane (solketal) and 2-butanol, respectively. It appears that entropic contributions to the stabilization of the enantioselectivity-determining transition state play an important role in the enantiopreference. Consequences of these findings for the formulation of models that can be used to summarise the observed enantioselectivities are discussed.

KW - Acetobacter pasteurianus

KW - Comamonas testosteroni

KW - Enantioselectivity

KW - Enthalpy

KW - Entropy

KW - Oxidation

KW - Quinohaemoprotein alcohol dehydrogenase

KW - Temperature

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DO - https://doi.org/10.3109/10242429909040114

M3 - Article

SN - 1024-2422

VL - 17

SP - 179

EP - 207

JO - Biocatalysis and Biotransformation

JF - Biocatalysis and Biotransformation

IS - 3

ER -

Machado SS, Jongejan A, Geerlof A, Jongejan JA, Duine JA. Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols. Biocatalysis and Biotransformation. 1999;17(3):179-207. doi: https://doi.org/10.3109/10242429909040114

Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenases from Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols

Abstract

Keywords

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