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V-51 NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases

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pubpVHPO_revised.pdf (550.4Kb)
Date
02/04/2009
Author
Geethalakshmi, K. R.
Waller, Mark P.
Thiel, Walter
Buehl, Michael
Keywords
Fungus curvularia-inaequalis
Active-site mutants
Electronic-structure
Basis-sets
Dependent haloperoxidase
Catalytic mechanism
Ascophyllum-nodosum
Hydrogen-peroxide
Chloroperoxidase
Complexes
QD Chemistry
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Abstract
QM/MM models of the peroxo forms of vanadium-containing haloperoxidases (VHPOs) are critically assessed in terms of active site geometries, hydrogen bonds within the active site, isotropic and anisotropic V-51 NMR chemical shifts, and TD-DFT excitation energies. The geometric stability within the active site of the protein is comparable to the respective native forms, as indicated by low standard deviations in bond lengths across a number of local minima sampled along MID trajectories. There is a significant calculated upfield shift in delta(V-51) upon formation of the peroxo from the respective native forms for both the vanadium-containing chloroperoxidase (VCPO) and vanadium-containing bromoperoxidase (VBPO) models, which is in qualitative agreement with V-51 NMR experiments of VBPO in solution. The models show appreciable differences between the anisotropic chemical shifts of the different protonation states of the peroxo form of VHPO. The most likely candidates for the peroxo forms of the VHPO enzymes appear to be unprotonated or have a single proton on either of the equatorial oxygen ligands, based on QM/MM modeling in combination with X-ray, V-51 NMR, and UV-vis data.
Citation
Geethalakshmi , K R , Waller , M P , Thiel , W & Buehl , M 2009 , ' V-51 NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases ' , Journal of Physical Chemistry B , vol. 113 , no. 13 , pp. 4456-4465 . https://doi.org/10.1021/jp8109308
Publication
Journal of Physical Chemistry B
Status
Peer reviewed
DOI
https://doi.org/10.1021/jp8109308
ISSN
1520-6106
Type
Journal article
Rights
This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry B, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see DOI: 10.1021/jp8109308
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  • University of St Andrews Research
URI
http://hdl.handle.net/10023/1757

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