Extended Data Fig. 6: Reactivity profile of cysteine residues involved in Fe-S ligation.
From: Monitoring Fe–S cluster occupancy across the E. coli proteome using chemoproteomics
a, Proteomic workflow for measuring the cysteine reactivity of Fe-S cluster ligands in an iron-depleted E. coli proteome labeled with 100 µM IA-Light or 10 µM IA-Heavy. b, Cysteine reactivity curve for all quantified cysteine residues (light gray) from an iron-depleted E. coli proteome (see Supplementary Dataset 9). Fe-S cluster cysteine ligands are highlighted (green circles). c,d Violin plot of L/H ratios for unique groups of (c) functional cysteine residues, including Fe-S ligands (red), active site residues (blue), zinc ligands (purple), disulfides (green), and iron ligands (yellow) and (d) Fe-S ligands from Fe-S client proteins (red) and Fe-S scaffold proteins (yellow). The median R value for each functional group of cysteine residues is displayed as a dashed line, while the average R values (red) and number of unique values (black) are indicated for each group.
