Open AccessDistinct effect of xenobiotics on the metal‐binding properties of protein molecules
Author(s) -
Novikova Natalia,
Kovalchuk Mikhail,
Stepiina,
Gaynutdinov Radmir,
Chukhrai Elena,
Yurieva Eleonora
Publication year - 2015
Publication title -
journal of synchrotron radiation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 99
ISSN - 1600-5775
DOI - 10.1107/s1600577515005627
Subject(s) - xenobiotic , chemistry , molecule , metal ions in aqueous solution , metal , distilled water , alkaline phosphatase , inorganic chemistry , crystallography , biochemistry , enzyme , organic chemistry , chromatography
The X‐ray standing‐wave method was applied to study the elemental composition and molecular organization of ordered protein films of alkaline phosphatase exposed to different xenobiotics (drug compounds, lead). Binding of metal ions from triply distilled water to protein molecules has been experimentally observed. Definite differences in the arrangement of impurity metal ions in the films have been established. The considerable enhancement of protein–metal interactions is attributed to partial rearrangement of the protein native structure, induced by xenobiotics.