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. 2016 Oct;163:185–193. doi: 10.1016/j.jinorgbio.2016.07.013

Fig. 2.

Fig. 2

Stopped-flow kinetics of BcII-catalysed nitrocefin hydrolysis. A & B. Spectral changes during the reaction of 50 μM di-Zn(II) BcII, or di-Fe(II) BcII, respectively, with 50 μM nitrocefin in a 1:1 ratio at pH 7.5 and 5 °C. Difference spectra of absorbance wavelengths 300–750 nm from 0.3–1.2 s using absorbance at 0.3 s as a baseline. Arrows indicate growth or decay of peaks. C & D. Time course of the reaction of 50 μM di-Zn(II) BcII, or di-Fe(II) BcII, respectively, with 50 μM nitrocefin in a 1:1 ratio of enzyme to substrate at pH 7.5 and 5 °C. Absorbance traces at 390, 485 and 665 nm. Dashed lines indicate fitting curve traces.