MAO Visible Spectroscopy for Ligand Interactions, Redox Chemistry, and Kinetics of Irreversible Inhibition.
| Autor: | Ramsay RR; School of Biology, Biomolecular Sciences Research Complex, University of St Andrews, Fife, UK. rrr@st-andrews.ac.uk. |
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| Jazyk: | angličtina |
| Zdroj: | Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2023; Vol. 2558, pp. 63-74. |
| DOI: | 10.1007/978-1-0716-2643-6_6 |
| Abstrakt: | 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. (© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.) |
| Databáze: | MEDLINE |
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