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Fig. 7 | AMB Express

Fig. 7

From: Kinetic characterization of acetone monooxygenase from Gordonia sp. strain TY-5

Fig. 7

a Time-resolved absorbance spectra collected over 75 s following the re-oxidation of reduced GSTACMO (20 μM) in the presence 500 μM NADP+ with air-saturated buffer (50 mM HEPES pH 7.5, 20% glycerol). b The same experiment as performed as for panel A with the exception of 200 μM of butanone added to the air-saturated buffer. c Stopped-flow single wavelength traces at 366 nm following rapid mixing of reduced GSTACMO (20 μM) in the presence 500 μM NADP+ against air-saturated buffer (50 mM HEPES pH 7.5, 20% glycerol) with 200 μM of butanone (black circles) and without butanone (grey circles). Fitting the data to a single exponential equation gave observed rate constants of 6.5 ± 0.8 s−1 (with butanone) and 8.9 ± 0.2 s−1 (without butanone). d Stopped-flow single wavelength traces at 440 nm following rapid mixing of reduced GSTACMO (20 μM) in the presence 500 μM NADP+ against air-saturated 50 mM HEPES pH 7.5, 20% glycerol with 200 μM of butanone (black circles) and without butanone (grey circles). The absorbance traces with butanone were fitted to a single exponential equation giving an observed rate constant of 0.80 ± 0.01 s−1, and the absorbance traces without butanone were fitted to a double exponential giving rate constants of 0.47 ± 0.01 s−1 and 0.06 ± 0.01 s−1

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