Origin of the Proton-transfer Step in the Cofactor-free (1H)-3-Hydroxy-4-oxoquinaldine 2,4-Dioxygenase

• Published in: The Journal of biological chemistry Vol. 289; no. 12; pp. 8620 - 8632
• Main Authors: Hernandez-Ortega, Aitor, Quesne, Matthew G., Bui, Soi, Heuts, Dominic P.H.M., Steiner, Roberto A., Heyes, Derren J., de Visser, Sam P., Scrutton, Nigel S.
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 01.03.2014
• Subjects: DFT Calculations; Enzyme Kinetics; Enzyme Mechanisms; Isotope Effects; Molecular Dynamics; Quantum Mechanics/Molecular Mechanics; Site-directed Mutagenesis; Enzyme Mechanisms; Site-directed Mutagenesis; Molecular Dynamics; Quantum Mechanics/Molecular Mechanics; DFT Calculations; Enzyme Kinetics; Isotope Effects

Dioxygenases catalyze a diverse range of chemical reactions that involve the incorporation of oxygen into a substrate and typically use a transition metal or organic cofactor for reaction. Bacterial (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) belongs to a class of oxygenases able to catalyz...