Issue 27, 2014

A DFT and ONIOM study of C–H hydroxylation catalyzed by nitrobenzene 1,2-dioxygenase

Abstract

A detailed description of the mechanism of C–H hydroxylation by Rieske non-heme iron dioxygenases remains elusive, as the nature of the oxidizing species is not definitively known. DFT calculations on cluster models of nitrobenzene 1,2-dioxygenase were done to explore possible mechanisms arising from oxidation by either the experimentally observed FeIII–OOH complex or the putative high-valent HO–FeV[double bond, length as m-dash]O intermediate formed through a heterolytic O–O bond cleavage. Hydrogen abstraction by HO–FeV[double bond, length as m-dash]O, followed by oxygen rebound, was found to be consistent with experimental studies. The findings from the quantum mechanical cluster approach were verified by accounting for the effect of the protein environment on transition state geometries and reaction barriers through ONIOM calculations.

Graphical abstract: A DFT and ONIOM study of C–H hydroxylation catalyzed by nitrobenzene 1,2-dioxygenase

Supplementary files

Article information

Article type
Paper
Submitted
10 Mar 2014
Accepted
19 May 2014
First published
19 May 2014
This article is Open Access
Creative Commons BY license

Phys. Chem. Chem. Phys., 2014,16, 13889-13899

Author version available

A DFT and ONIOM study of C–H hydroxylation catalyzed by nitrobenzene 1,2-dioxygenase

I. Geronimo and P. Paneth, Phys. Chem. Chem. Phys., 2014, 16, 13889 DOI: 10.1039/C4CP01030B

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