Elemental sulfur: Toxicity in vivo and in vitro to bacterial luciferase, in vitro yeast alcohol dehydrogenase, and bovine liver catalase
(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
- Cetkauskaite, A ; Pessala, P and Södergren, Anders LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Environmental Toxicology
- volume
- 19
- issue
- 4
- pages
- 372 - 386
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- wos:000223178800017
- pmid:15269910
- scopus:4444262585
- pmid:15269910
- ISSN
- 1520-4081
- DOI
- 10.1002/tox.20025
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Chemical Ecology/Ecotoxicology (Closed 2011) (011006020)
- id
- c9be85dd-f3fa-4491-8b1a-541f51033f7a (old id 135833)
- date added to LUP
- 2016-04-01 12:33:59
- date last changed
- 2022-01-27 06:49:40
@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 Inc.}},
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}},
doi = {{10.1002/tox.20025}},
volume = {{19}},
year = {{2004}},
}