Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula.
作者： Jacob H. Artz , Spencer N. White , Oleg A. Zadvornyy , Corey J. Fugate , Danny Hicks
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摘要: Mercuric ion reductase (MerA), a mercury detoxification enzyme, has been tuned by evolution to have high specificity for mercuric ions (Hg2+) and catalyze their reduction more volatile, less toxic elemental form. Here, we present biochemical structural characterization of MerA from the thermophilic crenarchaeon Metallosphaera sedula. M. sedula is thermostable remains active after extended incubation at 97 °C. At 37 ᵒC, NADPH oxidation-linked Hg2+ specific activity was found be 1.9 µmol/min•mg, increasing 3.1µmol/min•mg 70 crystals were obtained structure solved 1.6 A, representing first crystal MerA. Comparison both amino acid sequence mesophillic counterparts provides new insights into determinants that underpin thermal stability enzyme.
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