H2O2 selectively damages the binuclear iron-sulfur cluster N1b of respiratory complex I

• Published in: Scientific reports Vol. 13; no. 1; p. 7652
• Main Authors: Strotmann, Lisa, Harter, Caroline, Gerasimova, Tatjana, Ritter, Kevin, Jessen, Henning J., Wohlwend, Daniel, Friedrich, Thorsten
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 11.05.2023; Nature Publishing Group; Nature Portfolio
• Subjects: 631/45/173; 631/45/49; 631/45/535; 631/57/1464; 631/92/173; 631/92/603; 631/92/607; E coli; Electron transfer; Electron transport chain; Energy metabolism; Flavin mononucleotide; Humanities and Social Sciences; Hydrogen peroxide; Membranes; multidisciplinary; NADH-ubiquinone oxidoreductase; Oxidation; Physiology; Proteins; Reactive oxygen species; Science; Science (multidisciplinary); Spectrum analysis; Sulfur; Translocation; Ubiquinone oxidoreductase
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-023-34821-5

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 2 O 2 , 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.