PDBsum entry 4z40

Oxidoreductase

PDB id: 4z40

Contents

Protein chains

652 a.a.

166 a.a.

Ligands

UNX ×4

SF4 ×16

MTE-MTE

MTE ×6

Metals

_ZN ×4

__W ×4

_MG ×4

Waters ×139

PDB id:

4z40

Name:

Oxidoreductase

Title:

Active site complex bambc of benzoyl coenzyme a reductase as isolated

Structure:

Benzoyl-coa reductase, putative. Chain: a, b, c, d. Engineered: yes. Iron-sulfur cluster-binding oxidoreductase, putative benzoyl-coa reductase electron transfer protein. Chain: e, f, g, h. Engineered: yes

Source:

Geobacter metallireducens gs-15. Organism_taxid: 269799. Gene: bamb-1, gmet_2087. Expressed in: geobacter metallireducens. Expression_system_taxid: 269799. Gene: bamc-1, gmet_2086.

Resolution:

2.35Å R-factor: 0.213 R-free: 0.238

Authors:

T.Weinert,J.W.Kung,S.Weidenweber,S.G.Huwiler,M.Boll,U.Ermler

Key ref:

T.Weinert et al. (2015). Structural basis of enzymatic benzene ring reduction. Nat Chem Biol, 11, 586-591. PubMed id: 26120796 DOI: 10.1038/nchembio.1849

Date:

01-Apr-15 Release date: 24-Jun-15

Protein chains

Q39TV8  (Q39TV8_GEOMG) -  Benzoyl-CoA reductase, putative from Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15)

Seq: 653 a.a.

Struc: 652 a.a.

Protein chains

Q39TV9  (Q39TV9_GEOMG) -  Iron-sulfur cluster-binding oxidoreductase, putative benzoyl-CoA reductase electron transfer protein from Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15)

Seq: 179 a.a.

Struc: 166 a.a.

DOI no: 10.1038/nchembio.1849

Nat Chem Biol 11:586-591 (2015)

PubMed id: 26120796

Structural basis of enzymatic benzene ring reduction.

T.Weinert, S.G.Huwiler, J.W.Kung, S.Weidenweber, P.Hellwig, H.J.Stärk, T.Biskup, S.Weber, J.J.Cotelesage, G.N.George, U.Ermler, M.Boll.

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.