Article: The nature of the carbon dioxide substrate and equilibrium constant of the 6-phosphogluconate dehydrogenase reaction

1. It was shown that dissolved CO(2) and not HCO(3) (-) or H(2)CO(3) is the primary substrate for reductive carboxylation with 6-phosphogluconate dehydrogenase from sheep liver. 2. The equilibrium constant of the reaction was measured in solutions of various ionic strengths and at several temperatures, and the free energy and heat of reaction were determined.

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References

1.

Williamson D, Lund P, KREBS H . The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J. 1967; 103(2):514-27. PMC: 1270436. DOI: 10.1042/bj1030514. View

2.

Engel P, Dalziel K . The equilibrium constants of the glutamate dehydrogenase systems. Biochem J. 1967; 105(2):691-5. PMC: 1198365. DOI: 10.1042/bj1050691. View

3.

Londesborough J, Dalziel K . The equilibrium constant of the isocitrate dehydrogenase reaction. Biochem J. 1968; 110(2):217-22. PMC: 1187200. DOI: 10.1042/bj1100217. View

4.

Dalziel K, Londesborough J . The mechanisms of reductive carboxylation reactions. Carbon dioxide or bicarbonate as substrate of nicotinamide-adenine dinucleotide phosphate-linked isocitrate dehydrogenase and malic enzyme. Biochem J. 1968; 110(2):223-30. PMC: 1187201. DOI: 10.1042/bj1100223. View

5.

Veech R, EGGLESTON L, KREBS H . The redox state of free nicotinamide-adenine dinucleotide phosphate in the cytoplasm of rat liver. Biochem J. 1969; 115(4):609-19. PMC: 1185185. DOI: 10.1042/bj1150609a. View

6.

Villet R, Dalziel K . Purification and properties of 6-phosphogluconate dehydrogenase from sheep liver. Biochem J. 1969; 115(4):639-43. PMC: 1185188. DOI: 10.1042/bj1150639. View

7.

DISCHE Z, Borenfreund E . A new spectrophotometric method for the detection and determination of keto sugars and trioses. J Biol Chem. 1951; 192(2):583-7. View

8.

Burton K, KREBS H . The free-energy changes associated with the individual steps of the tricarboxylic acid cycle, glycolysis and alcoholic fermentation and with the hydrolysis of the pyrophosphate groups of adenosinetriphosphate. Biochem J. 1953; 54(1):94-107. PMC: 1268852. DOI: 10.1042/bj0540094. View

9.

SRERE P, Cooper J, Tabachnick M, RACKER E . The oxidative pentose phosphate cycle. I. Preparation of substrates and enzymes. Arch Biochem Biophys. 1958; 74(2):295-305. DOI: 10.1016/0003-9861(58)90001-8. View

10.

Klingenberg M, BUECHER T . Biological oxidations. Annu Rev Biochem. 1960; 29:669-708. DOI: 10.1146/annurev.bi.29.070160.003321. View

11.

Dalziel K . Kinetic studies of liver alcohol dehydrogenase. Biochem J. 1962; 84:244-54. PMC: 1243656. DOI: 10.1042/bj0840244. View

The Nature of the Carbon Dioxide Substrate and Equilibrium Constant of the 6-phosphogluconate Dehydrogenase Reaction