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

Fumiaki Takeuchi, Kenji Iwahori, Kazuo Kamimura, Tsuyoshi Sugio

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Abstract

Fifty iron-oxidizing bacteria isolated from natural environments were screened for resistance to mercuric ions (Hg2+). Thiobacillus ferrooxidans Funis 2-1, the strain found to show the greatest resistance to Hg2+ among the fifty isolates, gave a cell yield of 7.0 x 107 cells/ml after 8 d cultivation in an Fe2+-medium (pH 2.5) containing 0.7 μM Hg2+. Funis 2-1 volatilized 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 μM Hg2+ even over a 28 d cultivation period. When resting cells of strains Funis 2-1 and AP19-3 were incubated for 3 h in a salt solution containing 0.7 μM Hg2+ (pH 3.0), 14.3% and 7.9% of the total mercury added to the reaction mixtures respectively, were 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 markedly higher mercury resistance of Funis 2-1 compared with that of AP19-3 cannot be explained only by the level of the mercuric reductase activity, the levels of mercury resistance of iron oxidase and cytochrome c oxidase were studied. The 1 μM mercuric ions inhibited the 35% of iron- oxidizing activity 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 μM Hg2+ inhibited approximately 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 μM Hg2+. Since cytochrome c oxidase is one of the most important components of the iron- oxidizing system, 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 responsible for the more rapid growth of Funis 2-1 than that of in an Fe2+-medium containing 0.7 μM Hg2+.

Original languageEnglish
Pages (from-to)387-392
Number of pages6
JournalJournal of Bioscience and Bioengineering
Volume88
Issue number4
DOIs
Publication statusPublished - 1999

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Thiobacillus
Mercury (metal)
Mercury
Innate Immunity
Electron Transport Complex IV
Iron
Oxidoreductases
Enzymes
Ions
Cytochromes c
Bacteria
Salts
Proteins
Growth
mercuric reductase

Keywords

  • Iron-oxidizing bacterium
  • Mercuric reductase
  • Mercury resistance
  • Thiobacillus ferrooxidans

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering

Cite this

@article{19f732bc788e4cd9b18c4c83d15e858c,
title = "Isolation and some properties of Thiobacillus ferrooxidans strains with differing levels of mercury resistance from natural environments",
abstract = "Fifty iron-oxidizing bacteria isolated from natural environments were screened for resistance to mercuric ions (Hg2+). Thiobacillus ferrooxidans Funis 2-1, the strain found to show the greatest resistance to Hg2+ among the fifty isolates, gave a cell yield of 7.0 x 107 cells/ml after 8 d cultivation in an Fe2+-medium (pH 2.5) containing 0.7 μM Hg2+. Funis 2-1 volatilized 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 μM Hg2+ even over a 28 d cultivation period. When resting cells of strains Funis 2-1 and AP19-3 were incubated for 3 h in a salt solution containing 0.7 μM Hg2+ (pH 3.0), 14.3{\%} and 7.9{\%} of the total mercury added to the reaction mixtures respectively, were 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 markedly higher mercury resistance of Funis 2-1 compared with that of AP19-3 cannot be explained only by the level of the mercuric reductase activity, the levels of mercury resistance of iron oxidase and cytochrome c oxidase were studied. The 1 μM mercuric ions inhibited the 35{\%} of iron- oxidizing activity 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 μM Hg2+ inhibited approximately 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 μM Hg2+. Since cytochrome c oxidase is one of the most important components of the iron- oxidizing system, 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 responsible for the more rapid growth of Funis 2-1 than that of in an Fe2+-medium containing 0.7 μM Hg2+.",
keywords = "Iron-oxidizing bacterium, Mercuric reductase, Mercury resistance, Thiobacillus ferrooxidans",
author = "Fumiaki Takeuchi and Kenji Iwahori and Kazuo Kamimura and Tsuyoshi Sugio",
year = "1999",
doi = "10.1016/S1389-1723(99)80215-1",
language = "English",
volume = "88",
pages = "387--392",
journal = "Journal of Bioscience and Bioengineering",
issn = "1389-1723",
publisher = "The Society for Biotechnology, Japan",
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TY - JOUR

T1 - Isolation and some properties of Thiobacillus ferrooxidans strains with differing levels of mercury resistance from natural environments

AU - Takeuchi, Fumiaki

AU - Iwahori, Kenji

AU - Kamimura, Kazuo

AU - Sugio, Tsuyoshi

PY - 1999

Y1 - 1999

N2 - Fifty iron-oxidizing bacteria isolated from natural environments were screened for resistance to mercuric ions (Hg2+). Thiobacillus ferrooxidans Funis 2-1, the strain found to show the greatest resistance to Hg2+ among the fifty isolates, gave a cell yield of 7.0 x 107 cells/ml after 8 d cultivation in an Fe2+-medium (pH 2.5) containing 0.7 μM Hg2+. Funis 2-1 volatilized 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 μM Hg2+ even over a 28 d cultivation period. When resting cells of strains Funis 2-1 and AP19-3 were incubated for 3 h in a salt solution containing 0.7 μM Hg2+ (pH 3.0), 14.3% and 7.9% of the total mercury added to the reaction mixtures respectively, were 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 markedly higher mercury resistance of Funis 2-1 compared with that of AP19-3 cannot be explained only by the level of the mercuric reductase activity, the levels of mercury resistance of iron oxidase and cytochrome c oxidase were studied. The 1 μM mercuric ions inhibited the 35% of iron- oxidizing activity 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 μM Hg2+ inhibited approximately 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 μM Hg2+. Since cytochrome c oxidase is one of the most important components of the iron- oxidizing system, 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 responsible for the more rapid growth of Funis 2-1 than that of in an Fe2+-medium containing 0.7 μM Hg2+.

AB - Fifty iron-oxidizing bacteria isolated from natural environments were screened for resistance to mercuric ions (Hg2+). Thiobacillus ferrooxidans Funis 2-1, the strain found to show the greatest resistance to Hg2+ among the fifty isolates, gave a cell yield of 7.0 x 107 cells/ml after 8 d cultivation in an Fe2+-medium (pH 2.5) containing 0.7 μM Hg2+. Funis 2-1 volatilized 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 μM Hg2+ even over a 28 d cultivation period. When resting cells of strains Funis 2-1 and AP19-3 were incubated for 3 h in a salt solution containing 0.7 μM Hg2+ (pH 3.0), 14.3% and 7.9% of the total mercury added to the reaction mixtures respectively, were 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 markedly higher mercury resistance of Funis 2-1 compared with that of AP19-3 cannot be explained only by the level of the mercuric reductase activity, the levels of mercury resistance of iron oxidase and cytochrome c oxidase were studied. The 1 μM mercuric ions inhibited the 35% of iron- oxidizing activity 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 μM Hg2+ inhibited approximately 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 μM Hg2+. Since cytochrome c oxidase is one of the most important components of the iron- oxidizing system, 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 responsible for the more rapid growth of Funis 2-1 than that of in an Fe2+-medium containing 0.7 μM Hg2+.

KW - Iron-oxidizing bacterium

KW - Mercuric reductase

KW - Mercury resistance

KW - Thiobacillus ferrooxidans

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U2 - 10.1016/S1389-1723(99)80215-1

DO - 10.1016/S1389-1723(99)80215-1

M3 - Article

VL - 88

SP - 387

EP - 392

JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

SN - 1389-1723

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