Apparent Equilibrium Constants and Standard Transformed Gibbs Energies of Biochemical Reactions Involving Carbon Dioxide
- 1 December 1997
- journal article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 348 (1) , 116-124
- https://doi.org/10.1006/abbi.1997.0403
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- Thermodynamics of Enzyme-Catalyzed Reactions: Part 5. Isomerases and LigasesJournal of Physical and Chemical Reference Data, 1995
- Standard Transformed Formation Properties of Carbon Dioxide in Aqueous Solutions at Specified pHThe Journal of Physical Chemistry, 1995
- Recommendations for nomenclature and tables in biochemical thermodynamics (IUPAC Recommendations 1994)Pure and Applied Chemistry, 1994
- Thermodynamics of Reactions of Nicotinamide Adenine Dinucleotide and Nicotinamide Adenine Dinucleotide PhosphateArchives of Biochemistry and Biophysics, 1993
- Thermodynamics of Enzyme-Catalyzed Reactions: Part 1. OxidoreductasesJournal of Physical and Chemical Reference Data, 1993
- Standard thermodynamic formation properties for the adenosine 5'-triphosphate seriesBiochemistry, 1992
- The nature of carbon dioxide substrate and equilibrium constant of the 6-phosphogluconate dehydrogenase reactionBiochemical Journal, 1969
- The equilibrium constant of the isocitrate dehydrogenase reactionBiochemical Journal, 1968