ArticleJournal of neural transmission (Vienna, Austria : 1996)2013
Computational modeling of the direct hydride transfer mechanism for the MAO catalyzed oxidation of phenethylamine and benzylamine: ONIOM (QM/QM) calculations.
Article in Journal of neural transmission (Vienna, Austria : 1996), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 59 citations in OpenAlex.
- Article
- Oxidation of Flavin by Molecular Oxygen: Computational Insights into a Possible Radical Mechanism.ACS omega · 2024Article
- Article
- Computational insights on the hydride and proton transfer mechanisms of L-proline dehydrogenase.PloS one · 2023Article
- Brunner syndrome caused by point mutation explained by multiscale simulation of enzyme reaction.Scientific reports · 2022Article
- Computational Insights into β-Carboline Inhibition of Monoamine Oxidase A.Molecules (Basel, Switzerland) · 2022Article
- Why Monoamine Oxidase B Preferably MetabolizesInternational journal of molecular sciences · 2022Article
- Computational Analysis of the Nicotine Oxidoreductase Mechanism by the ONIOM Method.ACS omega · 2021Article
- Mechanistic study of L-6-hydroxynicotine oxidase by DFT and ONIOM methods.Journal of molecular modeling · 2021Article
- How Monoamine Oxidase A Decomposes Serotonin: An Empirical Valence Bond Simulation of the Reactive Step.The journal of physical chemistry. B · 2020Article
- Kinetics, mechanism, and inhibition of monoamine oxidase.Journal of neural transmission (Vienna, Austria : 1996) · 2018Review
- Evidence for a Cyanine Link Between Propargylamine Drugs and Monoamine Oxidase Clarifies the Inactivation Mechanism.Frontiers in chemistry · 2018Article
- The Use of Multiscale Molecular Simulations in Understanding a Relationship between the Structure and Function of Biological Systems of the Brain: The Application to Monoamine Oxidase Enzymes.Frontiers in neuroscience · 2016Review
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2 authors at 1 institution in 1 country.
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Abstract
Monoamine oxidases are two isozymic flavoenzymes which are the important targets for drugs used in the treatment of depression, Parkinson and Alzheimer's diseases. The catalytic reaction taking place between the cofactor FAD and amine substrate is still not completely understood. Herein we employed quantum chemical methods on the recently proposed direct hydride transfer mechanism including full active site residues of MAO isoforms in the calculations. Activation free energy barriers of direct hydride transfer mechanism for MAO-A and MAO-B were calculated by ONIOM (our own n-layered integrated molecular orbital + molecular mechanics) method with QM/QM (quantum mechanics:quantum mechanics) approach employing several density functional theory functionals, B3LYP, WB97XD, CAM-B3LYP and M06-2X, for the high layer. The formation of very recently proposed αC-flavin N5 adduct inside the enzyme has been investigated. ONIOM (M06-2X/6-31+G(d,p):PM6) results revealed that such an adduct may form only in MAO-B suggesting slightly different hydride transfer mechanisms for MAO-A and MAO-B.
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