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. 2014 Jan 24;53(6):1051–1058. doi: 10.1021/bi4016814

Figure 4.

Figure 4

Time courses of stopped-flow fluorescence experiments to measure either the kinetics of binding of MgFTP to (a) wild-type RePC and (b) mutant H216N or the kinetics of dissociation of (c) the wild-type RPC·MgFTP complex and (d) the H216N·MgFTP complex on displacement by MgATP. Reactions were performed at 30 °C. For panels a and b, 20 μM MgFTP was present in one syringe and 1 μM enzyme in the other. For panels c and d, 20 μM MgFTP and 1 μM wild-type RePC or H216N were present in one syringe and 2 mM MgATP was present in the other. Other reaction conditions were as described in Experimental Procedures.