Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation

Yumi Abiko, Eiko Yoshida, Isao Ishii, Jon M. Fukuto, Takaaki Akaike, Yoshito Kumagai

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Bismethylmercury sulfide (MeHg)<inf>2</inf>S has been found to be a detoxified metabolite of methylmercury (MeHg) that is produced by SH-SY5Y cells and in livers of rats exposed to MeHg. (MeHg)<inf>2</inf>S could be formed through the interactions between MeHg and sulfur species such as hydrogen sulfide (H<inf>2</inf>S or HS<sup>-</sup>), but the origin of its sulfur has not been fully identified. We herein examined the formation of (MeHg)<inf>2</inf>S through interactions between MeHg and persulfides, polysulfides, and protein preparations. Investigations using HPLC/atomic absorption spectrophotometry and EI-MS revealed that NaHS and Na<inf>2</inf>S<inf>4</inf> react readily with MeHg to give (MeHg)<inf>2</inf>S, and similar results were found using GSH persulfide (GSSH) formed endogenously or generated enzymatically in vitro. (MeHg)<inf>2</inf>S was also formed by incubation of MeHg with liver and heart cytosolic fractions prepared from wild-type mice but not with those from mice lacking cystathionine γ-lyase (CSE) that catalyzes the formation of cysteine persulfide. Consistent with this, (MeHg)<inf>2</inf>S was detected in a variety of tissues taken from wild-type mice intraperitoneally injected with MeHg in vivo but not in those from MeHg-injected CSE knockout mice. By separating liver fractions by column chromatography, we found numerous proteins that contain persulfides: one of the proteins was identified as being glutathione S-transferase pi 1. These results indicate that the formation of (MeHg)<inf>2</inf>S can be attributed to interactions between MeHg and endogenous free persulfide species, as well as protein-bound cysteine persulfide.

Original languageEnglish
Pages (from-to)1301-1306
Number of pages6
JournalChemical Research in Toxicology
Volume28
Issue number6
DOIs
Publication statusPublished - 2015 Jun 15

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Sulfides
Cystathionine
Liver
Lyases
Sulfur
Proteins
Glutathione S-Transferase pi
Atomic Spectrophotometry
Hydrogen Sulfide
Column chromatography
Spectrophotometry
Metabolites
Knockout Mice
Chromatography
Rats
High Pressure Liquid Chromatography
Tissue
persulfides
cysteine persulfide

ASJC Scopus subject areas

  • Toxicology

Cite this

Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation. / Abiko, Yumi; Yoshida, Eiko; Ishii, Isao; Fukuto, Jon M.; Akaike, Takaaki; Kumagai, Yoshito.

In: Chemical Research in Toxicology, Vol. 28, No. 6, 15.06.2015, p. 1301-1306.

Research output: Contribution to journalArticle

Abiko, Y, Yoshida, E, Ishii, I, Fukuto, JM, Akaike, T & Kumagai, Y 2015, 'Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation', Chemical Research in Toxicology, vol. 28, no. 6, pp. 1301-1306. https://doi.org/10.1021/acs.chemrestox.5b00101
Abiko, Yumi ; Yoshida, Eiko ; Ishii, Isao ; Fukuto, Jon M. ; Akaike, Takaaki ; Kumagai, Yoshito. / Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation. In: Chemical Research in Toxicology. 2015 ; Vol. 28, No. 6. pp. 1301-1306.
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AB - Bismethylmercury sulfide (MeHg)2S has been found to be a detoxified metabolite of methylmercury (MeHg) that is produced by SH-SY5Y cells and in livers of rats exposed to MeHg. (MeHg)2S could be formed through the interactions between MeHg and sulfur species such as hydrogen sulfide (H2S or HS-), but the origin of its sulfur has not been fully identified. We herein examined the formation of (MeHg)2S through interactions between MeHg and persulfides, polysulfides, and protein preparations. Investigations using HPLC/atomic absorption spectrophotometry and EI-MS revealed that NaHS and Na2S4 react readily with MeHg to give (MeHg)2S, and similar results were found using GSH persulfide (GSSH) formed endogenously or generated enzymatically in vitro. (MeHg)2S was also formed by incubation of MeHg with liver and heart cytosolic fractions prepared from wild-type mice but not with those from mice lacking cystathionine γ-lyase (CSE) that catalyzes the formation of cysteine persulfide. Consistent with this, (MeHg)2S was detected in a variety of tissues taken from wild-type mice intraperitoneally injected with MeHg in vivo but not in those from MeHg-injected CSE knockout mice. By separating liver fractions by column chromatography, we found numerous proteins that contain persulfides: one of the proteins was identified as being glutathione S-transferase pi 1. These results indicate that the formation of (MeHg)2S can be attributed to interactions between MeHg and endogenous free persulfide species, as well as protein-bound cysteine persulfide.

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