PMID:10216869

Citation	Buc, J, Santini, CL, Giordani, R, Czjzek, M, Wu, LF and Giordano, G (1999) Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli. Mol. Microbiol. 32:159-68
Abstract	The trimethylamine N-oxide (TMAO) reductase of Escherichia coli is a molybdoenzyme that catalyses the reduction of the TMAO to trimethylamine (TMA) with a redox potential of +130 mV. We have successfully substituted the molybdenum with tungsten and obtained an active tungsto-TMAO reductase. Kinetic studies revealed that the catalytic efficiency of the tungsto-substituted TMAO reductase (W-TorA) was increased significantly (twofold), although a decrease of about 50% in its kcat was found compared with the molybdo-TMAO reductase (Mo-TorA). W-TorA is more sensitive to high pH, is less sensitive to high NaCl concentration and is more heat resistant than Mo-TorA. Most importantly, the W-TorA becomes capable of reducing sulphoxides and supports the anaerobic growth of a bacterial host on these substrates. The evolutionary implication and mechanistic significance of the tungsten substitution are discussed.
Links	PubMed
Keywords	Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Kinetics; Molybdenum/metabolism; Mutagenesis; Oxidoreductases/metabolism; Oxidoreductases, N-Demethylating/chemistry; Oxidoreductases, N-Demethylating/isolation & purification; Oxidoreductases, N-Demethylating/physiology; Temperature; Time Factors; Tungsten/metabolism
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