XANES measurements for studies of adsorbed protein layers at liquid interfaces. / Konovalov, Oleg V.; Novikova, Natalia N.; Kovalchuk, Mikhail V.; Yalovega, Galina E.; Topunov, Alexey F.; Kosmachevskaya, Olga V.; Yurieva, Eleonora A.; Rogachev, Alexander V.; Trigub, Alexander L.; Kremennaya, Maria A.; Borshchevskiy, Valentin I.; Vakhrameev, Daniil D.; Yakunin, Sergey N.
In: Materials, Vol. 13, No. 20, 4635, 02.10.2020, p. 1-12.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - XANES measurements for studies of adsorbed protein layers at liquid interfaces
AU - Konovalov, Oleg V.
AU - Novikova, Natalia N.
AU - Kovalchuk, Mikhail V.
AU - Yalovega, Galina E.
AU - Topunov, Alexey F.
AU - Kosmachevskaya, Olga V.
AU - Yurieva, Eleonora A.
AU - Rogachev, Alexander V.
AU - Trigub, Alexander L.
AU - Kremennaya, Maria A.
AU - Borshchevskiy, Valentin I.
AU - Vakhrameev, Daniil D.
AU - Yakunin, Sergey N.
N1 - Publisher Copyright: © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2020/10/2
Y1 - 2020/10/2
N2 - 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.
AB - 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.
KW - Langmuir trough
KW - Metalloproteins
KW - Protein layers at liquid interface
KW - XANES
KW - Zinc binding sites
UR - http://www.scopus.com/inward/record.url?scp=85093848748&partnerID=8YFLogxK
U2 - 10.3390/ma13204635
DO - 10.3390/ma13204635
M3 - Article
AN - SCOPUS:85093848748
VL - 13
SP - 1
EP - 12
JO - Materials
JF - Materials
SN - 1996-1944
IS - 20
M1 - 4635
ER -
ID: 88197538