Details zur Publikation

Kategorie Textpublikation
Referenztyp Zeitschriften
DOI 10.1038/NCHEMBIO.1849
Volltext Shareable Link
Titel (primär) Structural basis of enzymatic benzene ring reduction
Autor Weinert, T.; Huwiler, S.G.; Kung, J.W.; Weidenweber, S.; Hellwig, P.; Stärk, H.-J.; Biskup, T.; Weber, S.; Cotelesage, J.J.H.; George, G.N.; Ermler, U.; Boll, M.
Journal / Serie Nature Chemical Biology
Erscheinungsjahr 2015
Department ANA
Band/Volume 11
Heft 8
Seite von 586
Seite bis 591
Sprache englisch
UFZ Querschnittsthemen RU4;
Abstract In chemical synthesis, the widely used Birch reduction of aromatic compounds to cyclic dienes requires alkali metals in ammonia as extremely low-potential electron donors. An analogous reaction is catalyzed by benzoyl–coenzyme A reductases (BCRs) that have a key role in the globally important bacterial degradation of aromatic compounds at anoxic sites. Because of the lack of structural information, the catalytic mechanism of enzymatic benzene ring reduction remained obscure. Here, we present the structural characterization of a dearomatizing BCR containing an unprecedented tungsten cofactor that transfers electrons to the benzene ring in an aprotic cavity. Substrate binding induces proton transfer from the bulk solvent to the active site by expelling a Zn2+ that is crucial for active site encapsulation. Our results shed light on the structural basis of an electron transfer process at the negative redox potential limit in biology. They open the door for biological or biomimetic alternatives to a basic chemical synthetic tool.
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Weinert, T., Huwiler, S.G., Kung, J.W., Weidenweber, S., Hellwig, P., Stärk, H.-J., Biskup, T., Weber, S., Cotelesage, J.J.H., George, G.N., Ermler, U., Boll, M. (2015):
Structural basis of enzymatic benzene ring reduction
Nat. Chem. Biol. 11 (8), 586 - 591