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Structural Properties of PQQ Involved in the Activity of Qiunohaemoprotein Alcohol Dehydrogenase from Pseudomonas Testosteroni

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Abstract

Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni was used in reconstitution experiments with PQQ and PQQ analogues to determine relevant factors contributing to binding and activity of PQQ. Preliminary results suggest the electrophilic properties of the C5-carbonyl group to be particularly important. For N1- and C8 -alkyl-substituted PQQ analogues a correlation of enzymatic activity and covalent hydration at C5 can be accounted for in terms of different conformations resulting from rotation of the C9-carboxyl group. Specific release of acetone from one enantiomer of racemic PQQ-acetone adduct upon incubation with apo-enzyme, suggests the presence of a nucleophilic group in the close vicinity of the PQQ-C5-carbonyl site in the enzyme. A mechanism for the dehydrogenation of aliphatic alcohols by quinohaemoprotein alcohol dehydrogenase from Pseudomonas testosteroni is presented.

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© 1989 Kluwer Academic Publishers

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Jongejan, J.A., Groen, B.W., Duine, J.A. (1989). Structural Properties of PQQ Involved in the Activity of Qiunohaemoprotein Alcohol Dehydrogenase from Pseudomonas Testosteroni . In: Jongejan, J.A., Duine, J.A. (eds) PQQ and Quinoproteins. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-0957-1_31

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  • DOI: https://doi.org/10.1007/978-94-009-0957-1_31

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6920-5

  • Online ISBN: 978-94-009-0957-1

  • eBook Packages: Springer Book Archive

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