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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Acknowledgements
We would like to thank Dr. B. Mark’s laboratory for assistance with column purification, V. Spicer and V. M. Collado for technical assistance in the mass spectrometry laboratory, and Drs. W. Ens and K. G. Standing for access to the mass spectrometers.
Funding
This work was supported by a NSERC Canada Discovery Grant and University of Manitoba GETS funds held by Dr. V. Yurkov and a University of Manitoba, Faculty of Science Scholarship awarded to C. Maltman.
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Communicated by Erko Stackebrandt.
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Maltman, C., Donald, L.J. & Yurkov, V. 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. Arch Microbiol 199, 1113–1120 (2017). https://doi.org/10.1007/s00203-017-1382-1
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DOI: https://doi.org/10.1007/s00203-017-1382-1