Isolation and some properties of Thiobacillus ferrooxidans strains with differing levels of mercury resistance from natural environments

Fifty iron-oxidizing bacteria isolated from natural environments were scree ned for resistance to mercuric ions (Hg2+). Thiobacillus ferrooxidans Funis 2-1, the strain found to show the greatest resistance to Hg2+ among the fi fty isolates, gave a cell yield of 7.0 x 10(7) cells/ml after 8 d cultivati on in an Fe2+-medium (pH 2.5) containing 0.7 mu M Hg2+. Funis 2-1 volatiliz ed 80% of the total mercury added to the medium over 8 d of cultivation. T. ferrooxidans AP19-3, more sensitive to Hg2+ than Funis 2-1, could not grow in an Fe2+-medium (pH 2.5) containing 0.7 mu M Hg2+ even over a 28 d culti vation period. When resting cells of strains Funis 2-1 and AP19-3 were incu bated for 3 h in a salt solution containing 0.7 mu M Hg2+ (pH 3.0), 14.3% a nd 7.9% of the total mercury added to the reaction mixtures respectively, w ere volatilized. The activity of the mercuric reductase from Funis 2-1 was only 2.8 times higher than that of the enzyme from AP19-3. Since the marked ly higher mercury resistance of Funis 2-1 compared with that of AP19-3 cann ot be explained only by the level of the mercuric reductase activity, the l evels of mercury resistance of iron oxidase and cytochrome c oxidase were s tudied. The 1 mu M mercuric ions inhibited the 35% of iron-oxidizing activi ty from AP19-3. In contrast, the same concentration of Hg2+ did not inhibit the activity of iron oxidase from Funis 2-1. In the case of the cytochrome c oxidases purified from both strains, the 0.2 mu M Hg2+ inhibited approxi mately 40% of cytochrome c oxidizing activity from AP19-3, on the contrary, the activity of the enzyme from Funis 2-1 was activated 1.8- and 1.2-fold, respectively, in the presence of 0.08 and 0.2 mu M Hg2+. Since cytochrome c oxidase is one of the most important components of the iron-oxidizing sys tem, these results indicate that both the existence of cytochrome c oxidase resistant to Hg2+ as well as that of mercuric reductase in the cells is re sponsible for the more rapid growth of Funis 2-1 than that of in an Fe2+-me dium containing 0.7 mu M Hg2+.