PURIFICATION AND CHARACTERIZATION OF THE SELENATE REDUCTASE FROM THAUERA SELENATIS

作者: Imke Schröder , Sabine Rech , Torsten Krafft , Joan M. Macy

DOI: 10.1074/JBC.272.38.23765

关键词: EnzymePeriplasmic spaceBiochemistryThauera selenatisSeleniumSelenateChemistryCofactorChlorateSelenate reductase

摘要: 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 to selenite catalyzed a reductase, previously shown be located in periplasmic space cell. This study describes purification enzyme from T. grown selenate. trimeric alphabetagamma complex an apparent Mr 180,000. alpha, beta, and gamma subunits are 96 kDa, 40 23 respectively, size. reductase contains molybdenum, iron, acid-labile sulfur prosthetic group constituents. UV-visible absorption spectroscopy also revealed presence cytochrome b per complex. Km for was determined 16 microM, Vmax micromol/min/mg protein. specific selenate; nitrate, nitrite, chlorate, sulfate were not reduced at detectable rates. These studies constitute first description which represents new class enzymes. significance this relation cell growth generation discussed.

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