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Dielectric barrier discharge plasma treatment affects stability, metal ion coordination, and enzyme activity of bacterial superoxide dismutases
Author(s) -
Krewing Marco,
Jung Christoph K.,
Dobbelstein Elena,
Schubert Britta,
Jacob Timo,
Bandow Julia E.
Publication year - 2020
Publication title -
plasma processes and polymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.644
H-Index - 74
eISSN - 1612-8869
pISSN - 1612-8850
DOI - 10.1002/ppap.202000019
Subject(s) - dielectric barrier discharge , superoxide dismutase , chemistry , superoxide , escherichia coli , enzyme , metal ions in aqueous solution , metal , active site , biochemistry , biophysics , organic chemistry , biology , electrode , gene
A molecular‐level understanding of the effects of atmospheric‐pressure plasma on biological samples requires knowledge of the effects on proteins. Superoxide dismutases, which detoxify superoxide under oxidative stress conditions, play a key role in bacterial plasma resistance. Investigation of the impact of dielectric barrier discharge (DBD) treatment on purified superoxide dismutases SodA and SodB of Escherichia coli showed that DBD treatment caused a rapid protein degradation, with only 8% of protein remaining after 10 min. The affinity of SodA for the metal cofactor Mn 2+ was reduced. Mass spectrometry, in conjunction with coupled‐cluster calculations, revealed that modifications of amino acid residues in the active site can explain the decreased metal affinity and a distortion of the coordination geometry responsible for the activity loss.