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. Author manuscript; available in PMC: 2009 Sep 2.
Published in final edited form as: Biochemistry. 2008 Aug 9;47(35):9227–9233. doi: 10.1021/bi801102e

Figure 3.

Figure 3

pH dependence of the conformational exchange kinetics in E:THF:NADP+ at 300 K. The rate constants for the excited-to-ground state transition (kBA) for the active-site loops, cofactor binding cleft and C-terminal associated region are plotted in red, green and blue, respectively. The dotted black curve is a simulation of the pH dependence of the hydride transfer rate constant with pKa 6.5 and pH-independent rate constant of 950 s−1 (at 298 K) (8).