Fig. 7: Simulations of the stopped-flow kinetic data for the reduction of roGFP2WT(S2). | Nature Communications

Fig. 7: Simulations of the stopped-flow kinetic data for the reduction of roGFP2WT(S2).

From: Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction

Fig. 7: Simulations of the stopped-flow kinetic data for the reduction of roGFP2WT(S2).

Simulation of the biphasic kinetic data for the reaction between 1 μM roGFP2WT(S2) and 1, 2.5, or 5 mM GSH in the presence of 1–40 µM reduced PfGrxC88S. Best fits (dashed lines) were obtained for a reaction within a ternary complex regardless whether (a) roGFP2(S2) or (b) GSH was first bound to PfGrx. Rounded rate constants from Table 1 in black were chosen as input parameters to calculate the missing parameters in blue. The relative fluorescence intensity of each roGFP2 redox species was taken from Fig. 2.

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