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. Author manuscript; available in PMC: 2019 Jan 1.
Published in final edited form as: Biochim Biophys Acta. 2017 May 1;1866(1):126–133. doi: 10.1016/j.bbapap.2017.04.003

Figure 3.

Figure 3

Optical spectra of d-camphor (1)-bound WT CYP101A (top), I160L/L166A (second down), I160L (third down) and I160L/L166F. Horizontal axes are wavelengths (nm), and vertical axes are absorptions. The top two (WT and I160L/L166A) both reduce nitrobenzophenone 6 to 7a (+NRase) and have a significant high-spin component (λmax= 390 nm) with camphor bound. The bottom two exhibit little or no high-spin state with camphor bound (low-spin (λmax = 390 nm) and neither show reductase activity towards 6 (-NRase).