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 215kDa comprised of 3 subunits (74, 42, and 25kDa) 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 5.6µmol/min/mg protein and a K m of 3.9mM. In the case of the tellurate reaction, V max and K m were 2.6µmol/min/mg protein and 2.6mM, respectively. Selenite reduction is carried out by another periplasmic enzyme with a V max of 2.8µmol/min/mg protein, K m of 12.1mM, and maximal activity at pH 6.0 and 38°C. This protein is 165kDa and comprised of 3 subunits of 98, 44, and 23kDa in a 1:1:1 ratio.
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