Summary
Quino(hemo)protein alcohol dehydrogenases, containing pyrroloquinoline quinone, PQQ as an organic cofactor, show appreciable enantioselectivity in the oxidation of chiral alcohols. Fundamental insight into the mechanistic and structural factors of importance for the observed enantio-selectivity has been obtained from the evaluation of the thermodynamic fingerprint of the kinetic features. It has been found that entropie contributions play a major role in the enantiopreference. Molecular modeling strategies, i.e. molecular mechanics and quantum mechanics calculations aimed at the evaluation of the Gibbs free energy difference between the enantioselectivity-controlling transition states have been developed. Preliminary results of deuterium kinetic isotope experiments appear relevant for the location of the transition states along the reaction coordinate.
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Jongejan, A., Jongejan, J.A. (2000). Enantioselectivity of PQQ-containing Alcohol Dehydrogenases: Kinetic, Thermodynamic, and Molecular Modeling. In: Iriarte, A., Martinez-Carrion, M., Kagan, H.M. (eds) Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8397-9_34
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DOI: https://doi.org/10.1007/978-3-0348-8397-9_34
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