Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance upgrade on Thursday 4th of May 2017 from 8.00am to 9.00am (BST).

During this time our websites will be offline temporarily. If you have any questions please use the feedback button on this page. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 27, 2014
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 10 Mar 2014, accepted on 19 May 2014 and first published on 19 May 2014


Article type: Paper
DOI: 10.1039/C4CP01030B
Citation: Phys. Chem. Chem. Phys., 2014,16, 13889-13899
  • Open access: Creative Commons BY license
  •   Request permissions

    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

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author