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Dielectric barrier discharge plasma treatment affects stability, metal ion coordination, and enzyme activity of bacterial superoxide dismutases

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 Mn2+ 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.

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Permanent Identifier (URI)
Is supplementing
Plasma Source Name
Plasma Source Application
Plasma Source Specification
Plasma Source Properties
V(RMS) = 13.5 kV, trigger frequency = 300 Hz, diameter=20 mm
English (United States)
Plasma Source Procedure
Aqueous sample of 40 μl on stainless steel support placed on grounded support. Distance between sample and DBD was 1 mm.
Plasma Medium Name
Plasma Medium Properties
room temperature. no further control.
Plasma Target Name
Contact Name
Bandow, Julia E.
Plasma Target Properties
purified superoxide dismutase. Escherichia coli BW25113, either ∆sodA, ∆sodB, ∆sodC, or ∆sodA∆sodB, taken from KEIO collection. 40 μl sample
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Public Access Level
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