Standard transformed Gibbs energies of coenzyme A derivatives as functions of pH and ionic strength

Biophysical Chemistry

Volumn 104, Issue 1, 2003, Pages 327-334

  Alberty, Robert A ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Apparent equilibrium constants; Coenzyme A; Inverse Legendre transform; Standard Gibbs energies of formation; Standard transformed Gibbs energies

Indexed keywords

ACETYL COENZYME A; COENZYME A; COENZYME A GLUTATHIONE; MALYL COENZYME A; METHYLMALONYLCOENZYME A; OXALYL COENZYME A; SUCCINYL COENZYME A; UNCLASSIFIED DRUG;

ARTICLE; BIOTRANSFORMATION; CALCULATION; CATALYSIS; CATALYST; ENERGY; EQUILIBRIUM CONSTANT; IONIC STRENGTH; PH; PRIORITY JOURNAL; STANDARD;

EID: 0038016444     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00390-3     Document Type: Article

References (24)

1. Goldberg R.N., Tewari Y.B., Bell D., Fazio D.K., Anderson E. Thermodynamics of enzyme catalyzed reactions: part 1. oxidoreductases. J. Phys. Chem. Ref. Data. 22:1993;515-582.
2. Goldberg R.N., Tewari Y.B. Thermodynamics of enzyme catalyzed reactions: part 2. transferases. J. Phys. Chem. Ref. Data. 23:1994;547-617.
3. Goldberg R.N., Tewari Y.B. Thermodynamics of enzyme catalyzed reactions: part 3 hydrolases. J. Phys. Chem. Ref. Data. 23:1994;1035-1103.
4. Goldberg R.N., Tewari Y.B. Thermodynamics of enzyme catalyzed reactions: part 4 lyases. J. Phys. Chem. Ref. Data. 24:1995;1669-1698.
5. Goldberg R.N., Tewari Y.B. Thermodynamics of enzyme catalyzed reactions: part 5 isomerases and ligases. J. Phys. Chem. Ref. Data. 24:1995;1765-1801.
6. Goldberg R.N. Thermodynamics of enzyme catalyzed reactions: part 6 - update. J. Phys. Chem. Ref. Data. 28:(1999):1999;931-965.
7. Alberty R.A., Goldberg R.N. Calculation of thermodynamic formation properties for the ATP series at specified pH and pMg. Biochemistry. 31:1992;10610-10615.
8. Alberty R.A. Equilibrium calculations on systems of biochemical reactions. Biophys. Chem. 42:1992;117-131.
9. Alberty R.A. Calculation of transformed thermodynamic properties of biochemical reactants at specified pH and pMg. Biophys. Chem. 43:1992;239-254.
10. Alberty R.A. Calculation of standard transformed Gibbs energies and standard transformed enthalpies of biochemical reactants. Arch. Biochem. Biophys. 353:1998;116-130.
11. Alberty R.A. Effect of temperature on the standard transformed Gibbs energies of reactants at various pH and ionic strength and apparent equilibrium constants of biochemical reactions. J. Phys. Chem. B. 105:2001;7865-7870.
12. Wolfram Research, Inc., 100 World Trade Center, Champaign, IL 61820-7237.
13. Alberty R.A. Standard apparent reduction potentials for biochemical half reactions as a function of pH and ionic strength. Arch. Biochem. Biophys. 389:2001;94-109.
14. R.A. Alberty, BasicBiochemData2 (2002), httpwwwmathsource.com/cgi-bin/msitem? 0211-622.
15. R.A. Alberty, Thermodynamics of Biochemical Reactions, Wiley, Hoboken, NJ, in press.
16. Callen H.B. Thermodynamics and an Introduction to Thermostatics. 1985;Wiley, Hoboken, NJ.
17. Alberty R.A. Inverse Legendre transform in biochemical thermodynamics: Applied to the last five reactions of glycolysis. J. Phys. Chem. 106B:2002;6594-6599.
18. Webb E.V. Enzyme Nomenclature. 1992;New York, Academic Press.
19. Guynn R.W., Webster L.T. Jr, Veech R.L. Equilibrium constants of the reactions of acetyl-CoA synthetase: The hydrolysis of adenosine triphosphate to amp and inorganic pyrophosphate. J. Biol. Chem. 249:1974;3248.
20. Lynn R., Guynn R.W. Equilibrium constants under physiological conditions for the reactions of succinyl coenzyme A synthetase and the hydrolysis of succinyl coenzyme A to coenzyme A and succinate. J. Biol. Chem. 253:1978;2546.
21. Qua J.R. Carbon assimilation by Pseudomanus oxalaticus (OK1): 6. Reactions of oxalyl-coenzyme A. Biochem. J. 87:1963;368.
22. Kellermeyer R.W., Allen S.H.G., Stjernholm R., Wood H.G. Methylmalonyl isomerase: purification and properties of the enzyme from propionibacteria. J. Biol. Chem. 239:1964;2562.
23. Hersh L.B. Malate adenosine triphosphate lyase. J. Biol. Chem. 248:1973;7295.
24. Chang S.H., Wilken D.R. Participation of the unsymmetrical disulfide of coA and glutathione in an enzymatic sulfhydryl disulfide interchange. J. Biol. Chem. 241:1966;425.