Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli.

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.

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@article{Buc1999EnzymaticAP, title={Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli.}, author={Jean Buc and C L Santini and Roger Giordani and Mirjam Czjzek and Long-Fei Wu and Girolamo Giordano}, journal={Molecular microbiology}, year={1999}, volume={32 1}, pages={159-68} }