Standard apparent reduction potentials of biochemical half reactions and thermodynamic data on the species involved.
Standard apparent reduction potentials E' degrees of half reactions of enzyme-catalyzed reactions are useful because they provide a global view of the apparent equilibrium constants of redox reactions. A table of E' degrees at a specified pH shows at a glance whether a given half reaction will drive another half reaction or be driven by it. This table can be used to calculate apparent equilibrium constants. Standard Gibbs energies of formation of species in a half reaction can be used to calculate E' degrees values at pHs in the range 5-9 and ionic strengths in the range of 0-0.35 M. My previously published values of E' degrees values for 42 half reactions has been extended by 22 new E' degrees values in this paper. When DeltafG degrees and DeltafH degrees are both known for all the species in an enzyme-catalyzed reaction at 298.15 K, it is possible to calculate all the standard transformed thermodynamic properties of the reaction over a range of pHs, ionic strengths, and temperatures.
Alberty
Robert A
RA
Department of Chemistry, Massachusetts Institute of Technology, 77 Mass. Ave., Cambridge, MA 02139, USA. alberty@mit.edu
D004735:Energy Transfer; D004798:Enzymes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008956:Models, Chemical; D010084:Oxidation-Reduction; D013696:Temperature; D013816:Thermodynamics
D004798:Enzymes