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.
authors.affiliation: Department of Inorganic Chemistry and Catalysis, Utrecht University, Utrecht, The Netherlands. ana_mijo@yahoo.com
authors.forename: Ana
authors.initials: A
authors.lastname: Mijovilovich
authors.forename: Sylvain
authors.initials: S
authors.lastname: Hamman
authors.forename: Fabrice
authors.initials: F
authors.lastname: Thomas
authors.forename: Frank M F
authors.initials: FM
authors.lastname: de Groot
authors.forename: Bert M
authors.initials: BM
authors.lastname: Weckhuysen
mesh_terms: D002256:Carbonic Anhydrases / Q000737:chemistry*; D020134:Catalytic Domain; D003300:Copper / Q000737:chemistry*; D005692:Galactose Oxidase / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D011522:Protons; D013052:Spectrometry, X-Ray Emission; D015032:Zinc / Q000737:chemistry*
chemical_list: D008024:Ligands; D011522:Protons; D003300:Copper; D005692:Galactose Oxidase; D002256:Carbonic Anhydrases; D015032:Zinc