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MAO Visible Spectroscopy for Ligand Interactions, Redox Chemistry, and Kinetics of Irreversible Inhibition

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Monoamine Oxidase

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2558))

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Abstract

The covalently bound FAD cofactor in monoamine oxidase (MAO) is reduced by the amine substrate and reoxidized by oxygen. Visible spectroscopy provides a convenient tool to study the interaction of ligands and the kinetics of the half-reactions for mechanistic investigations. Equilibrium redox titrations allow measurement of redox potentials, while rapid mixing experiments allow determination of the rate of reduction by different substrates and of covalent adduct formation by irreversible inactivators. Three techniques are described: (1) measuring ligand interactions by alterations in the spectrum, especially at 495 nm; (2) reducing MAO, including the essentials for anaerobic procedures; and (3) studying kinetics of reduction, reoxidation, or inactivation of MAO.

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Authors and Affiliations

  1. School of Biology, Biomolecular Sciences Research Complex, University of St Andrews, Fife, UK

    Rona R. Ramsay

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  1. Rona R. Ramsay
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Correspondence to Rona R. Ramsay .

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Editors and Affiliations

  1. Department of Biology and Biotechnology, University of Pavia, Pavia, Italy

    Claudia Binda

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Ramsay, R.R. (2023). MAO Visible Spectroscopy for Ligand Interactions, Redox Chemistry, and Kinetics of Irreversible Inhibition. In: Binda, C. (eds) Monoamine Oxidase. Methods in Molecular Biology, vol 2558. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2643-6_6

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  • DOI: https://doi.org/10.1007/978-1-0716-2643-6_6

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-2642-9

  • Online ISBN: 978-1-0716-2643-6

  • eBook Packages: Springer Protocols

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