Professor Robert A. Alberty--a legacy of excellence.

Professor Robert A. Alberty has created a legacy of excellence both in scientific research and in university education and administration. His career spans 67 years, during which time he has made many critical and seminal contributions in the areas of thermodynamics and kineticssthe vast majority of it dealing with biochemical reactions. The complexity of biochemical substances is largely attributable to the fact that a biochemical reactant is very often made up of a multiplicity of species. Thus, aqueous adenosine 5′triphosphate or ATP is generally a mixture of species such as ATP4-, HATP3-, H2ATP, Mg2ATP, MgATP2-, MgHATP-, CaATP2-, CaHATP-, etc. Alberty recognized this important fact early on and in the 1950s was one of the first to provide rigorous thermodynamic treatments to deal with it. Alberty’s papers published in 1968 and 1969 were the first to predict the complex dependency of the apparent equilibrium constant K′ and related quantities (∆rH′°, ∆rS′°, and ∆rCp′°) on pH, temperature, and the concentrations of other species such as free Mg2+ and Ca2+ for the hydrolysis of ATP, a very complex and important biochemical reaction. In particular, he developed Maxwell relationships that clearly demonstrate the interrelationships of the aforementioned quantities. He later applied numerical methods to solve the simultaneous nonlinear equations that are needed to describe the thermodynamics of biochemical reactions. He also developed and used the methods of isomer group thermodynamics and Legendre transforms to make fundamental progress in biochemical thermodynamics. In applying these methods, he provided a rigorous justification for the apparent equilibrium constant K′, the standard transformed Gibbs energy change ∆rG′°, the change in binding ∆rN(X) of a ligand X (e.g., X ) H+, Mg2+) in a biochemical reaction, as well as other transformed thermodynamic properties such as the standard apparent electromotive force E′°. Rigor and attention to detail were characteristic of Alberty’s publications. Alberty was one of the first to apply computer methods to problems in biochemical thermodynamics. During the past decade, he developed a useful set of computer codes as well as an extensive database for biochemical species and reactants. His methods have been applied to many complex biochemical systems such as the binding of oxygen to hemoglobin and even to entire metabolic pathways. His books Thermodynamics of Biochemical Reactions and Biochemical Thermodynamics: Applications of Mathematica are important to read for research scientists active in biochemical thermodynamics. At the beginning of the 1950s, the kinetic study of enzymecatalyzed reactions had barely advanced beyond the state in which Michaelis and his collaborators had left it more than thirty years earlier. The idea of a steady state had appeared, but studies of pH, inhibition, reactions of multiple substrates, temperature dependence, kinetics of isotope exchange, and fast reactions remained rudimentary. Alberty was one of a small number of scientists who realized that the subject was ripe for development, and he undertook the task with all the energy and enthusiasm that has characterized his whole career. Although others also made major contributions, he was probably the only one who has left his mark on every one of the aspects mentioned. J. Phys. Chem. B 2010, 114, 16045–16046 16045