Fig. 7: Effect of allosteric hPAS domain mutations.

a Absorption spectra of DosP^M30A under aerobic conditions (red), compared to anaerobic conditions (blue). b Turnover of 2 µM c-di-GMP at 25 °C by 10 nM aerobic DosP^M30A (red triangles), compared to anaerobic DosP^M30A (blue triangles) and CO-saturated DosP^M30A (orange squares). Each data point represents a measurement from an independent experiment (DosP^M30A aerobic and anaerobic n = 2. DosP^M30A with CO n = 1). c Absorption spectra of DosP^R131A under aerobic conditions (red), compared to anaerobic conditions (blue). d Turnover of 2 µM c-di-GMP at 25 °C by 10 nM aerobic DosP^R131A (red circles), compared to anaerobic DosP^R131A (blue circles). Each data point represents a measurement from an independent experiment (n = 2). For comparison, the enzymatic activities of aerobic DosP^WT (open squares, n = 2) and anaerobic DosP^WT (open triangles, n = 2) are re-plotted from Fig. 1g in b and d. e absorption spectra of DosP^M95I under aerobic conditions (red), compared to anaerobic conditions (blue). f Bar graph showing the k_cat values determined from the turnover of 2 µM c-di-GMP at 25 °C by 10 nM aerobic DosP^WT, DosP^M95I, DosP^R97A, DosP^M30A, and DosP^R131A. Values for DosP^WT and DosP^R97A are taken from Fig. 1. Other mutant values are the mean of two independent experiments with each individual experiment represented as a dot. The assay buffer was 20 mM Tris-HCl, 2.5 mM MgCl₂, 2.0 mM DTT, pH 8.0. Source data are provided as a Source Data file.