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Radiation chemists look at damage in redox proteins induced by X‐rays
Author(s) -
Wherland Scot,
Pecht Israel
Publication year - 2018
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25521
Subject(s) - radiolysis , redox , radical , chemistry , radiation damage , crystallization , aqueous solution , ion , metal ions in aqueous solution , metal , amino acid , protein crystallization , crystallography , irradiation , photochemistry , inorganic chemistry , biochemistry , organic chemistry , physics , nuclear physics
The three‐dimensional structure of proteins, especially as determined by X‐ray crystallography, is critical to the understanding of their function. However, the X‐ray exposure may lead to damage that must be recognized and understood to interpret the crystallographic results. This is especially relevant for proteins with transition metal ions that can be oxidized or reduced. The detailed study of proteins in aqueous solution by the technique of pulse radiolysis has provided a wealth of information on the production and fate of radicals that are the same as those produced by X‐ray exposure. The results reviewed here illustrate how the products of the interaction of radiation with water or with solutes added to the crystallization medium, and with proteins themselves, are formed, and about their fate. Of particular focus is how electrons are produced and transferred through the polypeptide matrix to redox centers such as metal ions or to specific amino acid residues, for example, disulfides, and how the hydroxyl radicals formed may be converted to reducing equivalents or scavenged.