title: Reverse-micelle model: pH, electromagnetic field and inhibitor enzyme interaction.
abstract: The reverse micelle is one of many models thought to have properties more nearly resembling the biological cellular environment, than does the traditional dilute-solution biochemical reaction system. In order to evaluate the results of EMF perturbation of enzyme-catalyzed reactions, the description of the AOT reverse-micelle model, with respect to its internal pH, effect of chemical inhibitors, temperature, and electromagnetic-field perturbation has herein been extended. Acetylcholinesterase and NADPH cytochrome-P450 reductase, reacting within the AOT reverse-micelle, exhibit a temperature vs. activity profile equivalent to the same reaction in a buffered dilute-solution environment. In reverse micelles, some inhibitors of AChE (propidium, and d-tubocurarine) have much less effect upon indophenol-acetate hydrolysis than they do in a dilute solution environment. Other inhibitors act in the same manner within the structured environment of the reverse micelle as in the conventional dilute solution reaction model. These differences are explicable in terms of mechanism of action of the individual inhibitors. Perturbation by low-intensity microwave fields has a similar inhibitory effect upon dilute-solution reactions, as those in the 'low-water-activity' environment of the reverse micelle. However, the interactions between physical and chemical perturbants are differently limited by the structure of the aqueous phase of the reverse micelle. pH of the 'internal' reverse-micelle environment is a function of the availability of H-ions supplied by system components. Use of indicator dyes show that the low-molarity buffers which are compatible with reverse-micelle stability, are often insufficient to maintain a constant pH. Too, in the reverse micelle, reaction rate, for proton yielding reactions, is dramatically greater than the rate of the same reaction in dilute solution at the same acidic pH.
authors.affiliation: Department of Biochemistry, NJAES, Rutgers University, New Brunswick, NJ 08903, USA.
authors.forename: S K
authors.initials: SK
authors.lastname: Chattopadhyay
authors.forename: K A
authors.initials: KA
authors.lastname: Toews
authors.forename: S
authors.initials: S
authors.lastname: Butt
authors.forename: R
authors.initials: R
authors.lastname: Barlett
authors.forename: H D
authors.initials: HD
authors.lastname: Brown
mesh_terms: D000818:Animals; D002021:Buffers; D002645:Chickens; D002746:Chlorpromazine / Q000494:pharmacology; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D004491:Edrophonium / Q000494:pharmacology; D004574:Electromagnetic Fields; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D008823:Micelles; D008872:Microwaves; D009251:NADPH-Ferrihemoprotein Reductase / Q000037:antagonists & inhibitors; D011419:Propidium / Q000494:pharmacology; D013696:Temperature; D014403:Tubocurarine / Q000494:pharmacology
chemical_list: D002021:Buffers; D002800:Cholinesterase Inhibitors; D004791:Enzyme Inhibitors; D008823:Micelles; D011419:Propidium; D004491:Edrophonium; D009251:NADPH-Ferrihemoprotein Reductase; D002746:Chlorpromazine; D014403:Tubocurarine