Protonation of the oxygen axial ligand in galactose oxidase model compounds as seen with high resolution X-ray emission experiments and FEFF simulations

A.E. Mijovilovich; Sylvain Hamman; Fabrice Thomas; Frank M. F. de Groot; Bert M. Weckhuysen

doi:10.1039/c0cp01144d

Protonation of the oxygen axial ligand in galactose oxidase model compounds as seen with high resolution X-ray emission experiments and FEFF simulations

A.E. Mijovilovich, Sylvain Hamman, Fabrice Thomas, Frank M. F. de Groot, Bert M. Weckhuysen

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

X-ray Emission Spectroscopy (XES) crossover peaks were shown to be sensitive to the protonation state of solvent molecules in the Zn protein carbonic anhydrase and its model compounds. Here we extend such studies to galactose oxidase models i.e. Cu(II) open d-shell systems, illustrating that XES combined with FEFF8 simulations reflect changes in the protonation state of the phenolate ligand for the copper center.

Original language	English
Pages (from-to)	5600-5604
Number of pages	5
Journal	Physical Chemistry Chemical Physics
Volume	13
Issue number	13
DOIs	https://doi.org/10.1039/c0cp01144d
Publication status	Published - 2011

Funding

B.M.W. and A. M. are grateful for the funding from NRSC-C and the Utrecht XAFS User Support group. We acknowledge the NSRRC synchrotron (Taiwan) for beamtime at the BL12XU beamline in SPring8 (Japan). Dr N. Hiraoka and Dr H. Ishii are kindly acknowledged for user support at SPring8, and Dr Jarridge. B. Hereijgers and Dr E. Suljoti from Utrecht University are acknowledged for their help during the synchrotron experiments. Computations were performed at SARA supercomputer facility (The Netherlands) under grant MP-06-124-VVV. The Physics Department of the University of Mar del Plata (Argentina) is acknowledged for providing a pleasant environment for writing this paper during the summer of 2009-2010.

Keywords

ABSORPTION SPECTROSCOPY
HISTIDINE COMPLEXES
CARBOXYLATE BINDING
RALSTONIA-EUTROPHA
SITE
EDGE
HYDROGENASE
SPECTRA
XANES

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title = "Protonation of the oxygen axial ligand in galactose oxidase model compounds as seen with high resolution X-ray emission experiments and FEFF simulations",

abstract = "X-ray Emission Spectroscopy (XES) crossover peaks were shown to be sensitive to the protonation state of solvent molecules in the Zn protein carbonic anhydrase and its model compounds. Here we extend such studies to galactose oxidase models i.e. Cu(II) open d-shell systems, illustrating that XES combined with FEFF8 simulations reflect changes in the protonation state of the phenolate ligand for the copper center.",

keywords = "ABSORPTION SPECTROSCOPY, HISTIDINE COMPLEXES, CARBOXYLATE BINDING, RALSTONIA-EUTROPHA, SITE, EDGE, HYDROGENASE, SPECTRA, XANES",

author = "A.E. Mijovilovich and Sylvain Hamman and Fabrice Thomas and \{de Groot\}, \{Frank M. F.\} and Weckhuysen, \{Bert M.\}",

year = "2011",

doi = "10.1039/c0cp01144d",

language = "English",

volume = "13",

pages = "5600--5604",

journal = "Physical Chemistry Chemical Physics",

issn = "1463-9076",

publisher = "Royal Society of Chemistry",

number = "13",

}

Protonation of the oxygen axial ligand in galactose oxidase model compounds as seen with high resolution X-ray emission experiments and FEFF simulations. / Mijovilovich, A.E.; Hamman, Sylvain; Thomas, Fabrice et al.
In: Physical Chemistry Chemical Physics, Vol. 13, No. 13, 2011, p. 5600-5604.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - Protonation of the oxygen axial ligand in galactose oxidase model compounds as seen with high resolution X-ray emission experiments and FEFF simulations

AU - Mijovilovich, A.E.

AU - Hamman, Sylvain

AU - Thomas, Fabrice

AU - de Groot, Frank M. F.

AU - Weckhuysen, Bert M.

PY - 2011

Y1 - 2011

N2 - X-ray Emission Spectroscopy (XES) crossover peaks were shown to be sensitive to the protonation state of solvent molecules in the Zn protein carbonic anhydrase and its model compounds. Here we extend such studies to galactose oxidase models i.e. Cu(II) open d-shell systems, illustrating that XES combined with FEFF8 simulations reflect changes in the protonation state of the phenolate ligand for the copper center.

AB - X-ray Emission Spectroscopy (XES) crossover peaks were shown to be sensitive to the protonation state of solvent molecules in the Zn protein carbonic anhydrase and its model compounds. Here we extend such studies to galactose oxidase models i.e. Cu(II) open d-shell systems, illustrating that XES combined with FEFF8 simulations reflect changes in the protonation state of the phenolate ligand for the copper center.

KW - ABSORPTION SPECTROSCOPY

KW - HISTIDINE COMPLEXES

KW - CARBOXYLATE BINDING

KW - RALSTONIA-EUTROPHA

KW - SITE

KW - EDGE

KW - HYDROGENASE

KW - SPECTRA

KW - XANES

U2 - 10.1039/c0cp01144d

DO - 10.1039/c0cp01144d

M3 - Article

SN - 1463-9076

VL - 13

SP - 5600

EP - 5604

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

IS - 13

ER -

Protonation of the oxygen axial ligand in galactose oxidase model compounds as seen with high resolution X-ray emission experiments and FEFF simulations

Abstract

Funding

Keywords

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