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. Author manuscript; available in PMC: 2009 Dec 4.
Published in final edited form as: Biochemistry. 2009 Feb 10;48(5):981–994. doi: 10.1021/bi801810h

Figure 7.

Figure 7

Reaction of BFDC with benzaldehyde monitored by stopped-flow PDA. (A) Difference spectra showing enamine formation from benzaldehyde. BFDC (33.3 μM concentration of active centers) in buffer B was mixed with an equal volume of 20 mM benzaldehyde in the same buffer at 30 °C. Reaction was monitored in the 300–595 nm wavelength range for 264 s, and spectra were recorded every 5 ms. (B) Rate of the enamine formation from benzaldehyde at 393 nm. Inset: Progress curve of enamine formation from benzaldehyde in the first 331 s. Data were fitted according to an equation for two enzyme states: P = y0 + ((υ1 − υ2)/k)(1 − e−kt) + υ2t, where υ1 and υ2 depict changes in A393 (ΔA · s−1) of two distinct enzyme states E1 and E2. The rate constant k pertains to the transition from E1 to E2. The values of the parameters are υ 1 = 0.91 × 10−5 ΔA · s−1, υ2 = 4.32 × 10−5 ΔA · s−1, y0 = 0.001 and k = 0.011 s−1.