Two distinct periplasmic enzymes are responsible for tellurite/tellurate and selenite reduction by strain ER-Te-48 associated with the deep sea hydrothermal vent tube worms at the Juan de Fuca Ridge black smokers

Abstract

Strain ER-Te-48 isolated from a deep-ocean hydrothermal vent tube worm is capable of resisting and reducing extremely high levels of tellurite, tellurate, and selenite, which are used for respiration anaerobically. Tellurite and tellurate reduction is accomplished by a periplasmic enzyme of 215 kDa comprised of 3 subunits (74, 42, and 25 kDa) in a 2:1:1 ratio. The optimum pH and temperature for activity is 8.0 and 35 °C, respectively. Tellurite reduction has a V _max of 5.6 µmol/min/mg protein and a K _m of 3.9 mM. In the case of the tellurate reaction, V _max and K _m were 2.6 µmol/min/mg protein and 2.6 mM, respectively. Selenite reduction is carried out by another periplasmic enzyme with a V _max of 2.8 µmol/min/mg protein, K _m of 12.1 mM, and maximal activity at pH 6.0 and 38 °C. This protein is 165 kDa and comprised of 3 subunits of 98, 44, and 23 kDa in a 1:1:1 ratio.

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