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The combined use of equilibrium and calorimetric measurements coupled with thermodynamic modeling calculations enables the characterization of the thermodynamics of enzyme-catalyzed reactions of interest to biochemistry and biotechnology. The information obtained allows for the prediction of the position of equilibrium of a variety of biochemical reactions over wide ranges of temperature, pH, and ionic strength. Some of the classes of reactions, which have been studied, include isomerization, hydrolysis, and phosphorylation of sugars, and ammonia and water elimination reactions. Many of the key industrial reactions including the conversion of trans-cinnamic acid and ammonia to L -phenylalanine, catalyzed by L -phenylalanine ammonia-lyase, and reactions involving penicillin and related antibiotics, have been studied with this methodology. Recent research has included studies of biochemical reactions in non-aqueous solvents including super-critical carbon dioxide and redox reactions. A series of comprehensive reviews of the thermodynamics of enzyme-catalyzed reactions have been completed. This database is available on the web: http://xpdb.nist.gov/enzyme_thermodynamics/ . Codes for performing equilibrium calculations on systems of biochemical reactions have also been developed and published: http://library.wolfram.com/infocenter/Articles/1620/ .
Expertise
- Calorimetry
- Chromatography
- Equilibrium modeling calculations
- Thermodynamic databases
Contacts
 
The apparent equilibrium constant K' for the hydrolysis
reaction (ATP + H 2 O = ADP + phosphate) as a function of
temperature T, pH, pMg, and ionic strength I.
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