NDLI: Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB*

Content Provider	PubMed Central
Author	Rather, Liv J. Weinert, Tobias Demmer, Ulrike Bill, Eckhard Ismail, Wael Fuchs, Georg Ermler, Ulrich
Copyright Year	2011
Abstract	The coenzyme A (CoA)-dependent aerobic benzoate metabolic pathway uses an unprecedented chemical strategy to overcome the high aromatic resonance energy by forming the non-aromatic 2,3-epoxybenzoyl-CoA. The crucial dearomatizing reaction is catalyzed by three enzymes, BoxABC, where BoxA is an NADPH-dependent reductase, BoxB is a benzoyl-CoA 2,3-epoxidase, and BoxC is an epoxide ring hydrolase. We characterized the key enzyme BoxB from Azoarcus evansii by structural and Mössbauer spectroscopic methods as a new member of class I diiron enzymes. Several family members were structurally studied with respect to the diiron center architecture, but no structure of an intact diiron enzyme with its natural substrate has been reported. X-ray structures between 1.9 and 2.5 Å resolution were determined for BoxB in the diferric state and with bound substrate benzoyl-CoA in the reduced state. The substrate-bound reduced state is distinguished from the diferric state by increased iron-ligand distances and the absence of directly bridging groups between them. The position of benzoyl-CoA inside a 20 Å long channel and the position of the phenyl ring relative to the diiron center are accurately defined. The C2 and C3 atoms of the phenyl ring are closer to one of the irons. Therefore, one oxygen of activated O2 must be ligated predominantly to this proximate iron to be in a geometrically suitable position to attack the phenyl ring. Consistent with the observed iron/phenyl geometry, BoxB stereoselectively should form the 2S,3R-epoxide. We postulate a reaction cycle that allows a charge delocalization because of the phenyl ring and the electron-withdrawing CoA thioester.
Related Links	http://dx.doi.org/10.1074/jbc.m111.236893
Ending Page	29248
Page Count	8
Starting Page	29241
File Format	PDF
ISSN	00219258
e-ISSN	1083351X
Journal	The Journal of Biological Chemistry
Issue Number	33
Volume Number	286
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2011-08-19
Access Restriction	Open
Rights Holder	American Society for Biochemistry and Molecular Biology
Subject Keyword	Cell Biology Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB

Coenzyme A-dependent Aerobic Metabolism of Benzoate via Epoxide Formation

A catalytically versatile benzoyl-CoA reductase, key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria

BENZOYL COENZYME A AND HIPPURATE SYNTHESIS

Palmitoyl-coenzyme A synthetase. Mechanism of reaction

Benzoyl and Hydroxybenzoyl Esters of Coenzyme A ULTRAVIOLET CHARACTERIZATION AND REACTION MECHANISMS

The Reaction Mechanism of Methyl-Coenzyme M Reductase

A product-inhibition study of the mechanism of mitochondrial octanoyl-coenzyme A synthetase

Mechanism of malonyl-coenzyme A-acyl-carrier protein transacylase.

Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB*

Similar Documents

Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB

Coenzyme A-dependent Aerobic Metabolism of Benzoate via Epoxide Formation

A catalytically versatile benzoyl-CoA reductase, key enzyme in the degradation of methyl- and halobenzoates in denitrifying bacteria

BENZOYL COENZYME A AND HIPPURATE SYNTHESIS

Palmitoyl-coenzyme A synthetase. Mechanism of reaction

Benzoyl and Hydroxybenzoyl Esters of Coenzyme A ULTRAVIOLET CHARACTERIZATION AND REACTION MECHANISMS

The Reaction Mechanism of Methyl-Coenzyme M Reductase

A product-inhibition study of the mechanism of mitochondrial octanoyl-coenzyme A synthetase

Mechanism of malonyl-coenzyme A-acyl-carrier protein transacylase.

Structure and Mechanism of the Diiron Benzoyl-Coenzyme A Epoxidase BoxB*