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Volume 272, Number 38, Issue of September 19, 1997 pp. 23765-23768
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Purification and Characterization of the Selenate Reductase from Thauera selenatis

(Received for publication, February 24, 1997, and in revised form, July 1, 1997)

Imke Schröder , Sabine Rech , Torsten Krafft ^§ and Joan M. Macy ^§

From the  Department of Microbiology and Molecular Genetics, University of California, Los Angeles, California 90095-1489 and the ^§ School of Microbiology, La Trobe University, Bundoora, Victoria, 3083 Australia

Thauera selenatis is one of two isolated bacterial species that can obtain energy by respiring anaerobically with selenate as the terminal electron acceptor. The reduction of selenate to selenite is catalyzed by a selenate reductase, previously shown to be located in the periplasmic space of the cell. This study describes the purification of the enzyme from T. selenatis grown anaerobically with selenate. The enzyme is a trimeric complex with an apparent M_r of 180,000. The , , and  subunits are 96 kDa, 40 kDa, and 23 kDa, respectively, in size. The selenate reductase contains molybdenum, iron, and acid-labile sulfur as prosthetic group constituents. UV-visible absorption spectroscopy also revealed the presence of one cytochrome b per complex. The K_m for selenate was determined to be 16 µM, and the V_max was 40 µmol/min/mg of protein. The enzyme is specific for the reduction of selenate; nitrate, nitrite, chlorate, and sulfate were not reduced at detectable rates. These studies constitute the first description of a selenate reductase, which represents a new class of enzymes. The significance of this enzyme in relation to cell growth and energy generation is discussed.

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