Maturation of iron-sulphur (Fe/S) proteins involves a complex biosynthetic machinery. Here we investigate the interaction of one component, Yah1, with its interaction partners apo-Isu1 and Nfs1-Isd11. Using anaerobic MicroScale Thermophoresis (MST) we show the redox dependency of the interaction between Yah1 and Isu1 as well as between Yah1 and Nfs1-Isd11. Reduced but not oxidized Yah1 tightly interacts with apo-Isu1 indicating a dynamic interaction between Yah1−apo-Isu1.
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