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Issue 34, 2019
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A detailed mechanism of the oxidative half-reaction of d-amino acid oxidase: another route for flavin oxidation

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Abstract

D-Amino acid oxidase (DAAO) is a flavoenzyme whose inhibition is expected to have therapeutic potential in schizophrenia. DAAO catalyses hydride transfer from the substrate to the flavin in the reductive half-reaction, and the flavin is reoxidized by O2 in the oxidative half-reaction. Quantum mechanical/molecular mechanical calculations were performed and their results together with available experimental information were used to elucidate the detailed mechanism of the oxidative half-reaction. The reaction starts with a single electron transfer from FAD to O2, followed by triplet–singlet transition. FAD oxidation is completed by a proton coupled electron transfer to the oxygen species and the reaction terminates with H2O2 formation by proton transfer from the oxidized substrate to the oxygen species via a chain of water molecules. The substrate plays a double role by facilitating the first electron transfer and by providing a proton in the last step. The mechanism differs from the oxidative half-reaction of other oxidases.

Graphical abstract: A detailed mechanism of the oxidative half-reaction of d-amino acid oxidase: another route for flavin oxidation

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Publication details

The article was received on 28 Apr 2019, accepted on 05 Aug 2019 and first published on 05 Aug 2019


Article type: Paper
DOI: 10.1039/C9OB00975B
Org. Biomol. Chem., 2019,17, 7973-7984

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    A detailed mechanism of the oxidative half-reaction of D-amino acid oxidase: another route for flavin oxidation

    D. J. Kiss and G. G. Ferenczy, Org. Biomol. Chem., 2019, 17, 7973
    DOI: 10.1039/C9OB00975B

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