4z40 | pdb_00004z40

Active site complex BamBC of Benzoyl Coenzyme A reductase as isolated

spinqualitylabelsall models 4z40, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4z40 is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, MTE, SF4, UNL, W, ZN Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Structural basis of enzymatic benzene ring reduction.,Weinert T, Huwiler SG, Kung JW, Weidenweber S, Hellwig P, Stark HJ, Biskup T, Weber S, Cotelesage JJ, George GN, Ermler U, Boll M Nat Chem Biol. 2015 Jun 29. doi: 10.1038/nchembio.1849. PMID:26120796 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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