Published September 1987 | Version v1
Journal article

Enzymatic methylation of sulfide, selenide, and organic thiols by Tetrahymena thermophila

  • 1. Univ. of Colorado, Boulder

Description

Cell extracts from the ciliate Tetrahymena thermophila catalyzed the S-adenosylmethionine-dependent methylation of sulfide. The product of the reaction, methanethiol, was detected by a radiometric assay and by a gas-chromatographic assay coupled to a sulfur-selective chemiluminescence detector. Extracts also catalyzed the methylation of selenide, and the product was shown by gas chromatography-mass spectrometry to be methaneselenol. The sulfide and selenide methyltransferase activities copurified with the aromatic thiol methyltransferase previously characterized from this organism, but heat inactivation experiments suggested the involvement of distinct sulfide and selenide methyltransferases. Short-term toxicity tests were carried out for sulfide, selenide, and their methylated derivatives; the monomethylated forms were somewhat more toxic than the nonmethylated or dimethylated compounds. Cell suspensions of T. thermophila exposed to sulfide, methanethiol, or their selenium analogs emitted methylated derivatives into the headspace. These results suggest that this freshwater protozoan is capable of the stepwise methylation of sulfide and selenide, leading to the release of volatile methylated sulfur or selenium gases

Additional details

Publishing Information

Journal Title
Appl. Environ. Microbiol.
Journal Volume
53
Journal Issue
9
Series
Appl. Environ. Microbiol.
Journal Page Range
2111-2118
ISSN
0099-2240
CODEN
AEMID