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Updated: Apr 10, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Modeling of the hydrophobic microenvironment of water-soluble molybdoenzymes in an aqueous micellar solution
Yuki Hasenaka1, Taka-aki Okamura, Kiyotaka Onitsuka
1Department of Macromolecular Science, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan. tokamura@chem.sci.osaka-u.ac.jp.
Abstract:
A toluene-soluble molybdenum(vi) complex containing a bulky hydrophobic substituent, (Et4N)2[Mo(VI)O2{1,2-S2-3,6-(RCONH)2C6H2}2] (R = (4-(t)BuC6H4)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.
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