Modeling of the hydrophobic microenvironment of water-soluble molybdoenzymes in an aqueous micellar solution

Abstract

A toluene-soluble molybdenum(VI) complex containing a bulky hydrophobic substituent, (Et₄N)₂[Mo^VIO₂{1,2-S₂-3,6-(RCONH)₂C₆H₂}₂] (R = (4-^tBuC₆H₄)₃C), was dissolved in the hydrophobic core of a micelle in an aqueous medium and catalyzed the biomimetic reduction of an amine N-oxide by an NADH analog. The kinetic isotope effect of solvent water clearly indicates that water molecules are essential for catalysis and are involved in the rate-determining step.