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Health, Safety & Environment

Ethylbenzene dehydrogenase

The first step in anaerobic ethylbenzene mineralization in denitrifying Azoarcus so. strain EB1 is the oxidation of ethylbenzene to (S)-(-)-1-phenylethanol. Ethylbenzene dehydrogenase, which catalyzes this reaction, is a unique enzyme in that it mediates the stereoselective hydroxylation of an aromatic hydrocarbon in the absence of molecular oxygen. Purified ethylbenzene dehydrogenase contains approximately 0.5 mol of molybdenum, 16 mol of iron, and 15 mol of acid-labile sulfur per mol of holoenzyme, and a molydopterin cofactor. According to sequence analysis and biochemical data ethylbenzene dehydrogenase is a novel member of the dimethyl sulfoxide reductase family of molybdopterin-containing enzymes.

Johnson, H.A., Pelletier, D. A., and Spormann, A. M., Isolation and characterization of anaerobic ethylbenzene dehydrogenase, a novel Mo-Fe-S enzyme, Journal of Bacteriology, 2001, 183, 4536-4542.

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