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Synchrotron Scattering Methods for Nanomaterials and Soft Matter Research
Open AccessArticle

XANES Measurements for Studies of Adsorbed Protein Layers at Liquid Interfaces

European Synchrotron Radiation Facility, 38043 Grenoble, France
National Research Center “Kurchatov Institute”, 123182 Moscow, Russia
Faculty of Physics, Southern Federal University, 344006 Rostov-on-Don, Russia
Bach Institute of Biochemistry, Federal Research Center of Biotechnology, Russian Academy of Sciences, 119071 Moscow, Russia
Veltischev Research and Clinical Institute for Paediatrics, Pirogov Russian National Research Medical University, 117997 Moscow, Russia
Moscow Institute of Physics and Technology, Dolgoprudny, 141701 Moscow Region, Russia
Author to whom correspondence should be addressed.
Materials 2020, 13(20), 4635;
Received: 31 August 2020 / Revised: 8 October 2020 / Accepted: 12 October 2020 / Published: 17 October 2020
(This article belongs to the Special Issue Advanced Synchrotron Techniques for Soft and Nanomaterials)
X-ray absorption near edge structure (XANES) spectra for protein layers adsorbed at liquid interfaces in a Langmuir trough have been recorded for the first time. We studied the parkin protein (so-called E3 ubiquitin ligase), which plays an important role in pathogenesis of Parkinson disease. Parkin contains eight Zn binding sites, consisting of cysteine and histidine residues in a tetracoordinated geometry. Zn K-edge XANES spectra were collected in the following two series: under mild radiation condition of measurements (short exposition time) and with high X-ray radiation load. XANES fingerprint analysis was applied to obtain information on ligand environments around zinc ions. Two types of zinc coordination geometry were identified depending on X-ray radiation load. We found that, under mild conditions, local zinc environment in our parkin preparations was very similar to that identified in hemoglobin, treated with a solution of ZnCl2 salt. Under high X-ray radiation load, considerable changes in the zinc site structure were observed; local zinc environment appeared to be almost identical to that defined in Zn-containing enzyme alkaline phosphatase. The formation of a similar metal site in unrelated protein molecules, observed in our experiments, highlights the significance of metal binding templates as essential structural modules in protein macromolecules. View Full-Text
Keywords: metalloproteins; XANES; zinc binding sites; protein layers at liquid interface; Langmuir trough metalloproteins; XANES; zinc binding sites; protein layers at liquid interface; Langmuir trough
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Konovalov, O.V.; Novikova, N.N.; Kovalchuk, M.V.; Yalovega, G.E.; Topunov, A.F.; Kosmachevskaya, O.V.; Yurieva, E.A.; Rogachev, A.V.; Trigub, A.L.; Kremennaya, M.A.; Borshchevskiy, V.I.; Vakhrameev, D.D.; Yakunin, S.N. XANES Measurements for Studies of Adsorbed Protein Layers at Liquid Interfaces. Materials 2020, 13, 4635.

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