4Z40

Active site complex BamBC of Benzoyl Coenzyme A reductase as isolated

Summary for 4Z40

• Entry DOI: 10.2210/pdb4z40/pdb
• Descriptor: Benzoyl-CoA reductase, putative, Iron-sulfur cluster-binding oxidoreductase, putative benzoyl-CoA reductase electron transfer protein, UNKNOWN LIGAND, ... (9 entities in total)
• Functional Keywords: aromatics, oxidoreductase, benzoyl-coa, anaerobic
• Biological source: Geobacter metallireducens GS-15; More
• Total number of polymer chains: 8
• Total formula weight: 386000.96

Authors

Weinert, T.,Kung, J.W.,Weidenweber, S.,Huwiler, S.G.,Boll, M.,Ermler, U. (deposition date: 2015-04-01, release date: 2015-06-24, Last modification date: 2024-01-10)

Primary citation

Weinert, T.,Huwiler, S.G.,Kung, J.W.,Weidenweber, S.,Hellwig, P.,Stark, H.J.,Biskup, T.,Weber, S.,Cotelesage, J.J.,George, G.N.,Ermler, U.,Boll, M.
Structural basis of enzymatic benzene ring reduction.
Nat.Chem.Biol., 11:586-591, 2015

PubMed 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 Zn(2+) 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.

PubMed: 26120796
DOI: 10.1038/nchembio.1849

Experimental method

X-RAY DIFFRACTION (2.35 Å)