期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 141, 期 17, 页码 6906-6914出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b12596
关键词
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资金
- Swiss National Science Foundation
- University of Basel
- Commission for Technology and Innovation, Professur fur Molekulare Bionik
- European Research Council [ERC-2013-StG 336559]
Ergothioneine is an emergent factor in cellular redox biochemistry in humans and pathogenic bacteria. Broad consensus has formed around the idea that ergothioneine protects cells against reactive oxygen species. The recent discovery that anaerobic microorganisms make the same metabolite using oxygen-independent chemistry indicates that ergothioneine also plays physiological roles under anoxic conditions. In this report, we describe the crystal structure of the anaerobic ergothioneine biosynthetic enzyme EanB from green sulfur bacterium Chlorobium limicola. This enzyme catalyzes the oxidative sulfurization of N-alpha-trimethyl histidine. On the basis of structural and kinetic evidence, we describe the catalytic mechanism of this unusual C-S bond-forming reaction. Significant active-site conservation among distant EanB homologues suggests that the oxidative sulfurization of heterocyclic substrates may occur in a broad range of bacteria.
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