ИСТИНА

Formate dehydrogenase (FDH, EC 1.2.1.2.) widespreads in nature and is found in many organisms like bacteria, yeasts, fungi and plants. FDH catalyses the reaction of NADH regeneration and plays a very significant role in vital functions, as it supplies the cell with energy in the form of NADH. FDH is also widely used for NADH regeneration in fine organic synthesis. Formate dehydrogenases from many different natural sources have been studied in our laboratory, and now a new FDH from Staphylococcus aureus (SauFDH) is one of our main interests. The genes, encoding two forms of SauFDH were successfully cloned and expressed in E. coli cells as active and soluble enzymes (SauFDH1 and SauFDH2). Our laboratory developed a method of obtaining recombinant FDHs, which led to producing sufficient amount of the enzymes. That fact allowed studying the main properties of new enzymes without unnecessary contacting the bacterium Staphylococcus aureus. The study of kinetic properties showed that SauFDH have rather high Michaelis constants both for formate and NAD+ compared to formate dehydrogenases from different other sources.. Since the FDH is responsible to this bacterium for life maintenance, its inhibition may cause energy starving and lead cell to death. Thus we decided to search for an appropriate inhibitor for this enzyme. In this work we present the data for inhibition of formate dehydrogenase from bacterium Staphylococcus aureus by several inorganic ions.