Work

Structural and Mechanistic Basis for Anaerobic Ergothioneine Biosynthesis

Year: 2019

Type: article

Abstract: 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-α-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.

Source: Journal of the American Chemical Society

DOI: 10.1021/jacs.8b12596

Authors: Florian Leisinger, Reto Burn, Marcel Meury, Peer Lukat, Florian P. Seebeck

Institutions: University of Basel, Helmholtz Centre for Infection Research

Language: English

Topic: Sulfur Compounds in Biology

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: Universität Basel, Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung, Kommission für Technologie und Innovation, FP7 Ideas: European Research Council

Award: Enzymology of oxidative sulfur transfers