4Z3Y: Active Site Complex Bambc Of Benzoyl Coenzyme A Reductase In Complex With Benzoyl-coa

Citation:
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.
PDB ID: 4Z3YDownload
MMDB ID: 130574
PDB Deposition Date: 2015/4/1
Updated in MMDB: 2015/07
Experimental Method:
x-ray diffraction
Resolution: 2.36  Å
Source Organism:
Similar Structures:
Biological Unit for 4Z3Y: octameric; determined by author and by software (PISA)
Molecular Components in 4Z3Y
Label Count Molecule
Proteins (8 molecules)
4
Benzoyl-coa Reductase, Putative
Molecule annotation
4
Iron-sulfur Cluster-binding Oxidoreductase, Putative Benzoyl-coa Reductase Electron Transfer Protein
Molecule annotation
Chemicals (40 molecules)
1
16
2
8
3
4
4
4
5
4
Molecule information is not avaliable.
6
4
* Click molecule labels to explore molecular sequence information.

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