tobias Weinert1,8, simona G Huwiler2,8, johannes W Kung2, sina Weidenweber1, petra Hellwig3,
Hans-joachim stärk4, till Biskup5, stefan Weber5, julien j H Cotelesage6,7, Graham n George6,
ulrich ermler1* & Matthias Boll2*
Nature Chemical Biology doi:10.1038/nchembio.1849
Received Accepted
Nature Chemical Biology doi:10.1038/nchembio.1849
Received Accepted
In chemical synthesis, the widely used Birch reduction of aromatic compounds to cyclic dienes requires alkali metals in ammo-
nia 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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