4Z3Y

Active site complex BamBC of Benzoyl Coenzyme A reductase in complex with Benzoyl-CoA

4Z3Y の概要

• エントリーDOI: 10.2210/pdb4z3y/pdb
• 分子名称: Benzoyl-CoA reductase, putative, Iron-sulfur cluster-binding oxidoreductase, putative benzoyl-CoA reductase electron transfer protein, IRON/SULFUR CLUSTER, ... (8 entities in total)
• 機能のキーワード: aromatics, reductase, benzoyl-coa, anaerobic, oxidoreductase
• 由来する生物種: Geobacter metallireducens GS-15; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 389225.88

構造登録者

Weinert, T.,Kung, J.W.,Weidenweber, S.,Huwiler, S.G.,Boll, M.,Ermler, U. (登録日: 2015-04-01, 公開日: 2015-07-01, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.359 Å)