SELENATE REDUCTASE: A MOLYBDENUM-CONTAINING ENZYME FROM THAUERA SELENATIS

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Selenate is an abundant oxyanion in some habitats, particularly in agricultural drainage waters from seleniferous soils. Organisms capable of reducing selenate to selenite and the less soluble elemental selenium are of interest as potential mediators of bioremediation. One organism capable of this is Thauera selenatis, using the enzyme selenate reductase. It is a periplasmic enzyme, consisting of three heterologous subunits at 100 kDa, 37 kDa and 23 kDa. It contains 1 mole of molybdenum, 12 moles of iron and 8 moles of acid-labile sulfur per mole of enzyme. This project aims to solve the structure of selenate reductase by the technique of multiple wavelength anomalous dispersion (MAD). X-ray diffraction data will be collected about the iron absorption edge and the anomalous differences used to determine phases.