Benzoyl-CoA Epoxidase of Azoarcus evansii
Published Online: 23 SEP 2013
Copyright © 2011 John Wiley & Sons, Ltd. All rights reserved.
Encyclopedia of Inorganic and Bioinorganic Chemistry
How to Cite
Weinert, T., Rather-Adler, L. J., Bill, E., Fuchs, G. and Ermler, U. 2013. Benzoyl-CoA Epoxidase of Azoarcus evansii. Encyclopedia of Inorganic and Bioinorganic Chemistry. 1–13.
- Published Online: 23 SEP 2013
Mineralization of aromatic compounds—present in large amounts in the biosphere—is a challenging chemical process. Nature developed several sophisticated degradation strategies, one of them being the benzoate-degrading CoA-linked Box pathway that is present in 5% of all sequenced bacterial genomes. The central dearomatization and cleavage reaction is accomplished by the BoxABC multicomponent system; BoxA is a reductase, BoxB an epoxidase using a single O2 molecule, and BoxC a stimulator for the BoxB reaction and a hydrolase for subsequent ring cleavage. BoxB is a member of the important diiron carboxylate protein family characterized by a catalytic diiron center embedded in a central four-helix bundle. Benzoyl-CoA is located inside a 20 Å long channel of BoxB. The position of its phenyl ring relative to the diiron center is accurately defined in the X-ray structure and allowed valuable insight into O2 binding and activation, epoxidation, and the stereoselectivity of the reaction. Kinetic- and electron paramagnetic resonance (EPR)-spectroscopic investigations provided information about the reaction dynamics and reaction intermediates. On the basis of the total data available, a detailed enzymatic mechanism is proposed.
- benzoate degradation;
- CoA ;
- Azoarcus evansii ;
- oxygen activation;
- BoxB ;