Fig. 2
UV–visible spectra and lauric acid (LA) conversion activity of CYP-Aa162 and CYP-Sm46Δ29 in the O2/redox partners/NAD(P)H system. a The UV–visible spectra are, respectively, shown for the substrate LA-bound ferric form of CYP-Sm46Δ29 with a Soret band at 422 nm (solid line); the CamAB/NADH ‘reduced’ CO-bound form of CYP-Sm46Δ29 with the Soret peak still at ~422 nm (dashed line); the substrate LA-bound ferric form of CYP-Aa162 with a Soret band at ~418 nm (dashed and dotted line); the CamAB/NADH ‘reduced’ CO-bound form of CYP-Aa162 with an unshifted Soret peak (dotted line). b Enzymatic conversion of lauric acid by CYP-Aa162, CYP-Sm46Δ29, and the control P450BM3 monooxygenase in the O2/redox proteins/NAD(P)H system in the absence or presence of different concentrations of catalase. For CYP-Aa162 and CYP-Sm46Δ29, CamAB/NADH was used for the electron transfer cascade. For the self-sufficient P450BM3 enzyme, NADPH was used as the electron donor. Conversions of the substrate in the H2O2 cofactor system were included as controls