Purification and Characterization of the Selenate Reductase from Thauera selenatis
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 cel...
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| Veröffentlicht in: | The Journal of biological chemistry 1997-09, Vol.272 (38), p.23765-23768 |
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| container_title | The Journal of biological chemistry |
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| creator | Schröder, Imke Rech, Sabine Krafft, Torsten Macy, Joan M. |
| description | 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 αβγ complex with an apparent Mrof 180,000. The α, β, and γ 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 αβγ complex. TheKm for selenate was determined to be 16 μm, and the Vmax 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. |
| doi_str_mv | 10.1074/jbc.272.38.23765 |
| format | Article |
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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 αβγ complex with an apparent Mrof 180,000. The α, β, and γ 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 αβγ complex. TheKm for selenate was determined to be 16 μm, and the Vmax 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. 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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 αβγ complex with an apparent Mrof 180,000. The α, β, and γ 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 αβγ complex. TheKm for selenate was determined to be 16 μm, and the Vmax 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. 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| ispartof | The Journal of biological chemistry, 1997-09, Vol.272 (38), p.23765-23768 |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Chromatography, Gel Electrophoresis, Polyacrylamide Gel Gram-Negative Facultatively Anaerobic Rods - enzymology Molecular Sequence Data Oxidoreductases - chemistry Oxidoreductases - isolation & purification Oxidoreductases - metabolism |
| title | Purification and Characterization of the Selenate Reductase from Thauera selenatis |
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