scholarly journals Water dynamics in small reverse micelles in two solvents: Two-dimensional infrared vibrational echoes with two-dimensional background subtraction

2011 ◽  
Vol 134 (5) ◽  
pp. 054512 ◽  
Author(s):  
Emily E. Fenn ◽  
Daryl B. Wong ◽  
M. D. Fayer
Keyword(s):  
Background Subtraction ◽  
Reverse Micelles ◽  
Water Dynamics ◽  
Two Dimensional

Geometry and Nanolength Scales versus Interface Interactions: Water Dynamics in AOT Lamellar Structures and Reverse Micelles

2009 ◽  
Vol 131 (23) ◽  
pp. 8318-8328 ◽  
Author(s):  
David E. Moilanen ◽  
Emily E. Fenn ◽  
Daryl Wong ◽  
M. D. Fayer
Keyword(s):  
Reverse Micelles ◽  
Water Dynamics ◽  
Lamellar Structures

scholarly journals A theoretical study on the expression of enzymic activity in reverse micelles

1989 ◽  
Vol 259 (2) ◽  
pp. 355-361 ◽  
Author(s):  
R Bru ◽  
A Sánchez-Ferrer ◽  
F Garcia-Carmona
Keyword(s):  
Reverse Micelle ◽  
Reverse Micelles ◽  
Structural Model ◽  
Dynamic Equilibrium ◽  
Free Water ◽  
Continuous Phase ◽  
Enzymic Activity ◽  
Water Dynamics ◽  
Polar Phase ◽  
Catalytic Constant

The present work deals with a theoretical model of catalysis by enzymes entrapped in reverse micelles. Three aspects of the enzyme-reverse-micelle system have been considered: structure, dynamics and enzyme distribution and catalysis in reverse micelles. A proposed structural model of reverse micelles [El Seoud (1984) in Reverse Micelles (Luisi, P. L. & Straub, B. E., eds.), p. 81, Plenum Press, New York] consists of three domains: surfactant apolar tails, bound water and free water. Dynamics are based on a dynamic equilibrium of association-dissociation that lead one to consider the dispersed polar phase as a pseudo-continuous phase [Luisi, Giomini, Pileni & Robinson (1988) Biochim. Biophys. Acta 947, 207-246]. Enzyme is distributed among the reverse-micelle domains and it expresses a catalytic constant for each one of them. The overall activity is calculated taking into account the volume in which enzyme is solubilized, and expressed as a function of the whole volume (V). The characteristic parameters of reverse micelles, omega 0 (= [H2O]/[surfactant]) and theta (= % water, v/v), were investigated as modulators of enzymic activity. Three basic patterns of modulation by omega 0 were found depending on which domain the enzyme expressed the highest catalytic constant. Combinations of those basic patterns lead to other modulation types that can be found experimentally, such as superactivation. Other combinations predict behaviour patterns not described to date, such as superinhibition. Dependence of catalytic activity on theta was only stated at omega 0 values around a critical value, which coincides with the appearance of free water.

scholarly journals Water Dynamics at the Interface in AOT Reverse Micelles

2009 ◽  
Vol 113 (25) ◽  
pp. 8560-8568 ◽  
Author(s):  
David E. Moilanen ◽  
Emily E. Fenn ◽  
Daryl Wong ◽  
M. D. Fayer
Keyword(s):  
Reverse Micelles ◽  
Water Dynamics ◽  
Aot Reverse Micelles
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