The long term objective is to increase the usefulness of equilibriumcalculations on biochemical reactions. Thermodynamics determine whether a reaction goes in the forward or reverse direction and whether it will absorb or evolve heat. More specifically, thermodynamics makes it possible to calculate equilibrium compositions and heat evolutions using data that often comes from other reactions. Knowledge of the thermodynamics of a reaction and knowledge of the kinetics of the forward reaction make it possible to calculate the kinetics of the reverse action. Chemical equilibrium in biological systems is complicated by the fact that apparent equilibrium constants depend on pH and pMg, as well as on temperature, pressure and ionic strength. A better understanding of these effects will facilitate the interpretation of metabolism and problems that are encountered in certain diseases. Thermodynamic information on biochemical reactions is currently stored as equilibrium constants and heats of specific reactions. These data can be interpreted by the use of recently developed techniques to obtain thermodynamic properties of individual reactants, which can then be used to calculate equilibrium constants and heats of reactions that have not even been studied previously. One objective of this project is to prepare thermodynamic tables on the properties of reactants so as to increase the usefulness of current knowledge. Another objective is to use new concepts in biochemical thermodynamics to investigate coupling of reactions by enzymes, missing reactions in systems like glycolysis, muscle, and chemosmotic theory.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM048358-02
Application #
2185832
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Project Start
1994-08-01
Project End
1997-07-31
Budget Start
1995-08-01
Budget End
1996-07-31
Support Year
2
Fiscal Year
1995
Total Cost
Indirect Cost
Name
Massachusetts Institute of Technology
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
Cambridge
State
MA
Country
United States
Zip Code
02139
Alberty, Robert A (2008) Rapid-equilibrium rate equations for the enzymatic catalysis of A+B=P+Q over a range of pH. Biophys Chem 132:114-26
Alberty, Robert A (2007) Thermodynamic properties of enzyme-catalyzed reactions involving cytosine, uracil, thymine, and their nucleosides and nucleotides. Biophys Chem 127:91-6
Alberty, Robert A (2007) Changes in binding of hydrogen ions in enzyme-catalyzed reactions. Biophys Chem 125:328-33
Alberty, Robert A (2006) Thermodynamic properties of weak acids involved in enzyme-catalyzed reactions. J Phys Chem B 110:5012-6
Alberty, Robert A (2006) Calculation of equilibrium compositions of systems of enzyme-catalyzed reactions. J Phys Chem B 110:24775-9
Alberty, Robert A (2006) Thermodynamics and kinetics of the glyoxylate cycle. Biochemistry 45:15838-43
Alberty, Robert A (2005) Thermodynamics of the mechanism of the nitrogenase reaction. Biophys Chem 114:115-20
Alberty, Robert A (2005) Calculation of thermodynamic properties of species of biochemical reactants using the inverse Legendre transform. J Phys Chem B 109:9132-9
Alberty, Robert A (2005) Thermodynamic properties of oxidoreductase, transferase, hydrolase, and ligase reactions. Arch Biochem Biophys 435:363-8
Alberty, Robert A (2005) Components and coupling in enzyme-catalyzed reactions. J Phys Chem B 109:2021-6

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