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Substrate structure governs maximum rate of catalysis exerted by cyclodextrin oxidase chemzymes

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Abstract

Selectively modified α- and β-cyclodextrin ketones or aldehydes act as artificial oxidases on a variety of small lipophilic substrates. The structure of the substrate is a highly important factor governing how effectively the oxidation reaction can be catalyzed. Amino acid-type substrates were not prone to catalysis, which yields new information about the limits of CD catalysis. Aniline showed some non-quantifiable catalysis, but for quinones and benzyl alcohols no net catalysis was detected. For aminophenol oxidation, o-aminophenols are far better substrates than p-aminophenols. The CD-catalyzed reaction follows Michaelis–Menten kinetics, involves CD cavity binding of the substrate and substrate recognition, and thus encompasses many of the hallmarks of natural enzymatic catalysis. Strong binding of the cooxidant H2O2 to the CD catalytic carbonyl group is a prerequisite for the subsequent oxidation of the substrate and in accordance with this, the binding of H2O2 to β-CD dialdehyde was shown to be strong (K d = 1.4 mM). β-CD 6A,6D-diketone which binds H2O2 weaker than an aldehyde was accordingly a less efficient oxidase. The wide range of substrates applicable to CD chemzyme catalysis brings about optimism for future scopes of synthetic biology.

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Fig. 1
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Abbreviations

CD:

Cyclodextrin

K m :

Michaelis–Menten constant

K d :

Dissociation constant

k cat :

Catalyzed reaction rate

k uncat :

Uncatalyzed reaction rate

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Acknowledgments

We thank The Lundbeck Foundation for financial support.

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Authors and Affiliations

  1. Department of Chemistry, University of Copenhagen, Copenhagen, Denmark

    Jeannette Bjerre & Mikael Bols

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  1. Jeannette Bjerre
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  2. Mikael Bols
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Correspondence to Mikael Bols.

Additional information

This work was presented at the First European Cyclodextrin Conference, Aalborg, Denmark, 11–13th of October 2009.

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Bjerre, J., Bols, M. Substrate structure governs maximum rate of catalysis exerted by cyclodextrin oxidase chemzymes. J Incl Phenom Macrocycl Chem 69, 417–423 (2011). https://doi.org/10.1007/s10847-010-9774-8

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