Robert N. Goldberg

Biochemical Science Division

NIST Building 227, Room A215
100 Bureau Drive
Gaithersburg, MD 20899-8312 USA
Phone: 301-975-2584
Email: robert.goldberg@nist.gov


 

Education

  • B.A. Chemistry, Johns Hopkins University, 1965
  • Ph.D. Physical Chemistry, Carnegie-Mellon University, 1969

 

Current Research

  • Biochemical Thermodynamics


Biochemical Thermodynamics

In general, apparent equilibrium constants K' and calorimetric enthalpies of reaction are the experimentally accessible quantities for biochemical reactions.  In most cases, K' is a function of temperature, pH, ionic strength, and the concentrations of ligands that bind to the substrates involved in the overall biochemical reaction.  If protons are absorbed or released in the overall biochemical reaction, the measured enthalpy will depend not only on the aforementioned quantities, but also on the enthalpy of ionization of the buffer used to carry out the reaction. Thus, it is necessary to develop thermodynamic models that can account for these complex and interrelated dependencies.  We have developed (R. N. Goldberg and Y. B. Tewari, "Thermodynamics of the disproportionation of adenosine 5'-diphosphate to adenosine 5'-triphosphate and adenosine 5'-monophosphate. I. Equilibrium model" Biophys. Chem. 1991, 40, 241- 261) models for the treatment of such data and continue to do research on such models.  Also, a Mathematica package "BioEqCalc" for treating complex equilibria in aqueous solutions has been developed.   Also, because the thermodynamic quantities of interest are state functions, results for a given reaction are interrelated to thermodynamic results for other reactions as well as to the properties of the substances involved in the reaction(s) of interest.  Thus, we also have an interest in thermochemical network calculations and in methods for the estimation of thermodynamic quantities. A recent publication ( Thermodynamic Database for Biological Buffers) reviews the status and gives selected values of thermodynamic quantities for the ionization reactions of 64 buffers, many of which are used in biochemistry.  Our database "Thermodynamics of Enzyme-Catalyzed Reactions" is available on the web.

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Publications

  • "Thermodynamics of enzyme-catalyzed reactions: Part 6 - 1999 update", RN Goldberg,  J. Phys. Chem. Ref. Data 28, 931-965 (1999).

  • "BioEqCalc:  A package for performing equilibrium calculations on biochemical reactions", DL Akers and RN Goldberg,  Mathematica J. 8, 1-30 (2001).

  • "Thermodynamic quantities for the ionization reactions of buffers in water", RN Goldberg, N Kishore, and RM Lennen,  J. Phys. Chem. Ref. Data 31, 231-370 (2002).

  • "Enzyme Catalysis - Thermodynamics," R. N. Goldberg, in the McGraw-Hill Yearbook of Science and Technology, McGraw-Hill, New York, 2003, pp. 111-114.

  • "Thermodynamics of the oxidation-reduction reaction {2 glutathionered(aq) + NADPox(aq) = glutathioneox(aq) + NADPred(aq)}," Y. B. Tewari and R. N. Goldberg, J. Chem. Thermodyn., 35, 1361-1381 (2003).

  • "Saturation molalities and standard molar enthalpies of solution of adenosine(cr), guanosine·2H2O(cr), inosine(cr), and xanthosine·2H2O(cr) in H2O(l)," Y. B. Tewari, R. Klein, M. D. Vaudin, and R. N. Goldberg, J. Chem. Thermodyn. 35, 1681-1702 (2003).

  • "Thermodynamics of the hydrolysis reactions of adenosine 3',5' (cyclic)phosphate(aq) and phosphoenolpyruvate(aq); the standard molar formation properties of 3',5' (cyclic)phosphate(aq) and phosphoenolpyruvate(aq)," R. N. Goldberg and Y. B. Tewari, J. Chem. Thermodyn. 35, 1809-1830 (2003).