title: Biochemical thermodynamics and rapid-equilibrium enzyme kinetics.
abstract: Biochemical thermodynamics is based on the chemical thermodynamics of aqueous solutions, but it is quite different because pH is used as an independent variable. A transformed Gibbs energy G' is used, and that leads to transformed enthalpies H' and transformed entropies S'. Equilibrium constants for enzyme-catalyzed reactions are referred to as apparent equilibrium constants K' to indicate that they are functions of pH in addition to temperature and ionic strength. Despite this, the most useful way to store basic thermodynamic data on enzyme-catalyzed reactions is to give standard Gibbs energies of formation, standard enthalpies of formation, electric charges, and numbers of hydrogen atoms in species of biochemical reactants like ATP. This makes it possible to calculate standard transformed Gibbs energies of formation, standard transformed enthalpies of formation of reactants (sums of species), and apparent equilibrium constants at desired temperatures, pHs, and ionic strengths. These calculations are complicated, and therefore, a mathematical application in a computer is needed. Rapid-equilibrium enzyme kinetics is based on biochemical thermodynamics because all reactions in the mechanism prior to the rate-determining reaction are at equilibrium. The expression for the equilibrium concentration of the enzyme-substrate complex that yields products can be derived by applying Solve in a computer to the expressions for the equilibrium constants in the mechanism and the conservation equation for enzymatic sites. In 1979, Duggleby pointed out that the minimum number of velocities of enzyme-catalyzed reactions required to estimate the values of the kinetic parameters is equal to the number of kinetic parameters. Solve can be used to do this with steady-state rate equations as well as rapid-equilibrium rate equations, provided that the rate equation is a polynomial. Rapid-equilibrium rate equations can be derived for complicated mechanisms that involve several reactants and various types of inhibitors, activators, and moderators.
authors.affiliation: Department of Chemistry, Massachusetts Institute of Technology, Room 6-215, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, United States. alberty@mit.edu
authors.forename: Robert A
authors.initials: RA
authors.lastname: Alberty
mesh_terms: D055162:Biocatalysis; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009994:Osmolar Concentration; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D004798:Enzymes; D014867:Water