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http://dx.doi.org/10.1136/bmj.4.5936.108-a | DOI Listing |
Allergol Int
January 2025
Institute of Allergology, Charité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Berlin, Germany; Fraunhofer Institute for Translational Medicine and Pharmacology ITMP, Immunology and Allergology, Berlin, Germany.
J Sex Med
January 2025
Department of Urology, University Vita-Salute San Raffaele, 20132 Milan, Italy.
J Sex Med
January 2025
Department of Urology, School of Medicine, Gazi University, 06560, Ankara, Turkiye.
Stroke Vasc Neurol
January 2025
Department of Neurosurgery, The First Hospital of China Medical University, Shenyang, Liaoning, China
J Mol Model
January 2025
Laboratorio de Química Teórica Computacional (QTC), Facultad de Química y de Farmacia, Pontificia Universidad Católica de Chile, Avenida Vicuña Mackenna 4860, 7820436, Santiago de Chile, Chile.
Context: Dopamine -monooxygenase (D M) is an essential enzyme in the organism that regioselectively converts dopamine into R-norepinephrine, the key step of the reaction, studied in this paper, is a hydrogen atom transfer (HAT) from dopamine to a superoxo complex on D M, forming a hydroperoxo intermediate and dopamine radical. It was found that the formation of a hydrogen bond between dopamine and the D M catalyst strengthens the substrate-enzyme interaction and facilitates the HAT which takes place selectively to give the desired enantiomeric form of the product. Six reactions leading to the hydroperoxo intermediate were analyzed in detail using theoretical and computational tools in order to identify the most probable reaction mechanism.
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