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Elemental sulfur: Toxicity in vivo and in vitro to bacterial luciferase, in vitro yeast alcohol dehydrogenase, and bovine liver catalase

Cetkauskaite, A; Pessala, P and Södergren, Anders LU (2004) In Environmental Toxicology 19(4). p.372-386
Abstract
The aim of this research was to analyze the effects and the modes of action of elemental sulfur (So) in bioluminescence and respiration of Vibrio fischeri cells and the enzymes crude luciferase, pure catalase, and alcohol dehydrogenase (ADH). Metallic copper removed sulfur and reduced the toxicity of acetone extracts of sediment samples analyzed in the bioluminescence test. The sulfur inhibition of cell bioluminescence was noncompetitive with decanal, the luciferase substrate; reversible, with maximum toxicity after 15 min (EC50 = 11.8 mug/L); and almost totally recovered after 2 h. In vitro preincubation of crude luciferase extract with sulfur (0.28 ppm) weakly inhibited bioluminescence at 5 min, but at 30 min the inhibition reached 60%.... (More)
The aim of this research was to analyze the effects and the modes of action of elemental sulfur (So) in bioluminescence and respiration of Vibrio fischeri cells and the enzymes crude luciferase, pure catalase, and alcohol dehydrogenase (ADH). Metallic copper removed sulfur and reduced the toxicity of acetone extracts of sediment samples analyzed in the bioluminescence test. The sulfur inhibition of cell bioluminescence was noncompetitive with decanal, the luciferase substrate; reversible, with maximum toxicity after 15 min (EC50 = 11.8 mug/L); and almost totally recovered after 2 h. In vitro preincubation of crude luciferase extract with sulfur (0.28 ppm) weakly inhibited bioluminescence at 5 min, but at 30 min the inhibition reached 60%. Increasing the concentration of sulfur in the parts per million concentration range in vitro decreased bioluminescence, which was not constant, but depended on exposure time, and no dead-end/total inhibition was observed. The redox state of enzymes in the in vitro system significantly affected inhibition. Hydrogen peroxide restored fully and the reducing agent dithiothreitol, itself toxic, restored only partially luciferase activity in the presence of sulfur. Sulfur (5.5 ppm) slightly inhibited ADH and catalase, and dithiothreitol enhanced sulfur inhibition. High sulfur concentrations (2.2 ppm) inhibited the bioluminescence and enhanced the respiration rate of V. fischeri cells. Elemental sulfur data were interpreted to show that sulfur acted on at least a few V. fischeri cell sites: reversibly modifying luciferase at sites sensitive to/protected by oxidative and reducing agents and by affecting electron transport processes, resulting in enhanced oxygen consumption. Sulfur together with an enzyme reducing agent inhibited the oxidoreductive enzymes ADH and catalase, which have -SH groups, metal ion cofactors, or heme, respectively, in their active centers.© 2004 Wiley Periodicals, Inc. Environ Toxicol 19: 372-386, 2004. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Environmental Toxicology
volume
19
issue
4
pages
372 - 386
publisher
John Wiley & Sons
external identifiers
  • wos:000223178800017
  • pmid:15269910
  • scopus:4444262585
ISSN
1520-4081
DOI
10.1002/tox.20025
language
English
LU publication?
yes
id
c9be85dd-f3fa-4491-8b1a-541f51033f7a (old id 135833)
date added to LUP
2007-06-27 09:10:40
date last changed
2017-01-01 05:15:28
@article{c9be85dd-f3fa-4491-8b1a-541f51033f7a,
  abstract     = {The aim of this research was to analyze the effects and the modes of action of elemental sulfur (So) in bioluminescence and respiration of Vibrio fischeri cells and the enzymes crude luciferase, pure catalase, and alcohol dehydrogenase (ADH). Metallic copper removed sulfur and reduced the toxicity of acetone extracts of sediment samples analyzed in the bioluminescence test. The sulfur inhibition of cell bioluminescence was noncompetitive with decanal, the luciferase substrate; reversible, with maximum toxicity after 15 min (EC50 = 11.8 mug/L); and almost totally recovered after 2 h. In vitro preincubation of crude luciferase extract with sulfur (0.28 ppm) weakly inhibited bioluminescence at 5 min, but at 30 min the inhibition reached 60%. Increasing the concentration of sulfur in the parts per million concentration range in vitro decreased bioluminescence, which was not constant, but depended on exposure time, and no dead-end/total inhibition was observed. The redox state of enzymes in the in vitro system significantly affected inhibition. Hydrogen peroxide restored fully and the reducing agent dithiothreitol, itself toxic, restored only partially luciferase activity in the presence of sulfur. Sulfur (5.5 ppm) slightly inhibited ADH and catalase, and dithiothreitol enhanced sulfur inhibition. High sulfur concentrations (2.2 ppm) inhibited the bioluminescence and enhanced the respiration rate of V. fischeri cells. Elemental sulfur data were interpreted to show that sulfur acted on at least a few V. fischeri cell sites: reversibly modifying luciferase at sites sensitive to/protected by oxidative and reducing agents and by affecting electron transport processes, resulting in enhanced oxygen consumption. Sulfur together with an enzyme reducing agent inhibited the oxidoreductive enzymes ADH and catalase, which have -SH groups, metal ion cofactors, or heme, respectively, in their active centers.© 2004 Wiley Periodicals, Inc. Environ Toxicol 19: 372-386, 2004.},
  author       = {Cetkauskaite, A and Pessala, P and Södergren, Anders},
  issn         = {1520-4081},
  language     = {eng},
  number       = {4},
  pages        = {372--386},
  publisher    = {John Wiley & Sons},
  series       = {Environmental Toxicology},
  title        = {Elemental sulfur: Toxicity in vivo and in vitro to bacterial luciferase, in vitro yeast alcohol dehydrogenase, and bovine liver catalase},
  url          = {http://dx.doi.org/10.1002/tox.20025},
  volume       = {19},
  year         = {2004},
}