Figure 3.

A, B) Normal mode associated to the substituents bending coupled to the hydride transfer in BsADH displayed as a superposition of two structures of the active site (red and blue) with benzyl alcohol (A) and isopropanol (B). C) The steady‐state rate constants (k _cat) for “light” (blue) and “heavy” (red) BsADH, and enzyme kinetic isotope effect (orange) from substrate A–G at 20 °C and pH 7.0. The substrates are: isopropanol (A), 2‐butanol (B), ethanol (C), 1‐pentanol (D), cyclopentanol (E), and cinnamyl (F) and benzyl (G) alcohols.