Skip to main content
. Author manuscript; available in PMC: 2017 Oct 4.
Published in final edited form as: Structure. 2016 Sep 1;24(10):1668–1678. doi: 10.1016/j.str.2016.07.012

Figure 2.

Figure 2

In solution kinetics of XcPrxQ. A. Bisubstrate kinetics of XcPrxQ (0.2 μM) with hydrogen peroxide and EcTrxA at 5 μM (black), 10 μM (red), 20 μM (green) and 40 μM (blue). The curves are the results of the global fitting of all four data sets. B. Same as A, but for cumene peroxide and EcTrxA at 5 μM (black), 10 μM (red), 20 μM (green) and 50 μM (blue). C–D. Time courses showing XcPrxQ hyperoxidative activity loss during reactions with varying concentrations (as indicated) of hydrogen peroxide and cumene hydroperoxide, respectively. E. The fraction of protein inactivated per turnover (Wood et al., 2003) (finact) is plotted as a function of peroxide concentration for XcPrxQ hyperoxidation by hydrogen peroxide (closed circles) and cumene peroxide (open circles). F. Sensitivity of XcPrxQ to hyperoxidation by hydrogen peroxide (closed circles) is compared to literature data (Nelson et al., 2013) for human PrxI (open squares) and Salmonella typhimurium AhpC (open circles). See also Table S2 and Table S3.