Proteomics of Desulfovibrio desulfuricans and X-ray absorption spectroscopy to investigate mercury methylation in the presence of selenium
(2014) In Metallomics 6(3). p.75-465- Abstract
The effects of mercury added as Hg(2+) and selenium as selenite to cultures of the sulfate reducing bacterium Desulfovibrio desulfuricans were investigated under controlled laboratory conditions. There was no significant difference in the growth curves in comparison to control except in the 0.5 μM Hg-6.3 μM Se combined system in which Hg methylation was significantly reduced. A significant decrease in the production of methylmercury indicates a disruption of the methylation process due to the presence of the relatively high concentrations of Se in the system, suggesting a modification of the biological pathway. The results of detailed 2D gel electrophoresis in combination with mass spectrometry confirmed that the Hg methylation process... (More)
The effects of mercury added as Hg(2+) and selenium as selenite to cultures of the sulfate reducing bacterium Desulfovibrio desulfuricans were investigated under controlled laboratory conditions. There was no significant difference in the growth curves in comparison to control except in the 0.5 μM Hg-6.3 μM Se combined system in which Hg methylation was significantly reduced. A significant decrease in the production of methylmercury indicates a disruption of the methylation process due to the presence of the relatively high concentrations of Se in the system, suggesting a modification of the biological pathway. The results of detailed 2D gel electrophoresis in combination with mass spectrometry confirmed that the Hg methylation process should certainly be influenced when the protein Dde_1198 protein-glutamate O-methyltransferase was totally suppressed in a culture containing 0.5 μM Hg and 6.3 μM Se. Since this protein plays an important role in the methylation process, its suppression in the presence of Se brings a possible explanation for the antagonism between Se and Hg in natural systems. The experiment involving the determination of Hg and Se in membrane proteins separated by 1D gel thin-layer isoelectric focusing revealed that when both elements were present in a culture, the concentration of Hg in the separated proteins was significantly lower in comparison to those without added Se to the culture and vice versa. Finally, near-edge X-ray absorption spectroscopy and extended X-ray absorption fine structure were used to corroborate the presence of a very inert solid HgSe in the cell membrane obtained from the culture containing 0.5 μM Hg and 6.3 μM Se. This confirms the protective effect of Se against Hg assimilation at the molecular level and reinforces the findings of our research group in numerous field and laboratory studies.
(Less)
- author
- Truong, Hoang-Yen Thi ; Chen, Yu-Wei ; Saleh, Mazen ; Nehzati, Susan LU ; George, Graham N ; Pickering, Ingrid J and Belzile, Nelson
- publishing date
- 2014-03
- type
- Contribution to journal
- publication status
- published
- keywords
- Bacterial Proteins/metabolism, Desulfovibrio desulfuricans/growth & development, Mercury/metabolism, Methylation, Methylmercury Compounds/metabolism, Methyltransferases/metabolism, Selenium/metabolism
- in
- Metallomics
- volume
- 6
- issue
- 3
- pages
- 11 pages
- publisher
- Oxford University Press
- external identifiers
-
- scopus:84896839234
- pmid:24413477
- ISSN
- 1756-5901
- DOI
- 10.1039/c3mt00323j
- language
- English
- LU publication?
- no
- id
- fbd08739-0d6f-4082-a0f4-6e24824af6bb
- date added to LUP
- 2020-02-07 14:47:59
- date last changed
- 2025-01-10 07:28:42
@article{fbd08739-0d6f-4082-a0f4-6e24824af6bb,
abstract = {{<p>The effects of mercury added as Hg(2+) and selenium as selenite to cultures of the sulfate reducing bacterium Desulfovibrio desulfuricans were investigated under controlled laboratory conditions. There was no significant difference in the growth curves in comparison to control except in the 0.5 μM Hg-6.3 μM Se combined system in which Hg methylation was significantly reduced. A significant decrease in the production of methylmercury indicates a disruption of the methylation process due to the presence of the relatively high concentrations of Se in the system, suggesting a modification of the biological pathway. The results of detailed 2D gel electrophoresis in combination with mass spectrometry confirmed that the Hg methylation process should certainly be influenced when the protein Dde_1198 protein-glutamate O-methyltransferase was totally suppressed in a culture containing 0.5 μM Hg and 6.3 μM Se. Since this protein plays an important role in the methylation process, its suppression in the presence of Se brings a possible explanation for the antagonism between Se and Hg in natural systems. The experiment involving the determination of Hg and Se in membrane proteins separated by 1D gel thin-layer isoelectric focusing revealed that when both elements were present in a culture, the concentration of Hg in the separated proteins was significantly lower in comparison to those without added Se to the culture and vice versa. Finally, near-edge X-ray absorption spectroscopy and extended X-ray absorption fine structure were used to corroborate the presence of a very inert solid HgSe in the cell membrane obtained from the culture containing 0.5 μM Hg and 6.3 μM Se. This confirms the protective effect of Se against Hg assimilation at the molecular level and reinforces the findings of our research group in numerous field and laboratory studies. </p>}},
author = {{Truong, Hoang-Yen Thi and Chen, Yu-Wei and Saleh, Mazen and Nehzati, Susan and George, Graham N and Pickering, Ingrid J and Belzile, Nelson}},
issn = {{1756-5901}},
keywords = {{Bacterial Proteins/metabolism; Desulfovibrio desulfuricans/growth & development; Mercury/metabolism; Methylation; Methylmercury Compounds/metabolism; Methyltransferases/metabolism; Selenium/metabolism}},
language = {{eng}},
number = {{3}},
pages = {{75--465}},
publisher = {{Oxford University Press}},
series = {{Metallomics}},
title = {{Proteomics of Desulfovibrio desulfuricans and X-ray absorption spectroscopy to investigate mercury methylation in the presence of selenium}},
url = {{http://dx.doi.org/10.1039/c3mt00323j}},
doi = {{10.1039/c3mt00323j}},
volume = {{6}},
year = {{2014}},
}