H 2 O 2 selectively damages the binuclear iron-sulfur cluster N1b of respiratory complex I

NADH:ubiquinone oxidoreductase, respiratory complex I, plays a major role in cellular energy metabolism by coupling electron transfer with proton translocation. Electron transfer is catalyzed by a flavin mononucleotide and a series of iron-sulfur (Fe/S) clusters. As a by-product of the reaction, the...

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Bibliographic Details
Published in:Scientific reports 2023-05, Vol.13 (1), p.7652
Main Authors: Strotmann, Lisa, Harter, Caroline, Gerasimova, Tatjana, Ritter, Kevin, Jessen, Henning J, Wohlwend, Daniel, Friedrich, Thorsten
Format: Article
Language:English
Subjects:
Electron Spin Resonance Spectroscopy
Electron Transport
Electron Transport Complex I - metabolism
Hydrogen Peroxide - metabolism
Iron - metabolism
Iron-Sulfur Proteins - metabolism
Oxidation-Reduction
Reactive Oxygen Species - metabolism
Sulfur - metabolism
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Summary:NADH:ubiquinone oxidoreductase, respiratory complex I, plays a major role in cellular energy metabolism by coupling electron transfer with proton translocation. Electron transfer is catalyzed by a flavin mononucleotide and a series of iron-sulfur (Fe/S) clusters. As a by-product of the reaction, the reduced flavin generates reactive oxygen species (ROS). It was suggested that the ROS generated by the respiratory chain in general could damage the Fe/S clusters of the complex. Here, we show that the binuclear Fe/S cluster N1b is specifically damaged by H O , however, only at high concentrations. But under the same conditions, the activity of the complex is hardly affected, since N1b can be easily bypassed during electron transfer.
ISSN:2045-2322