Difference between revisions of "Lehninger 1949 J Biol Chem"
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|journal=J Biol Chem | |journal=J Biol Chem | ||
|abstract=The oxidation of β-hydroxybutyrate to acetoacetate by molecular oxygen in a particulate fraction of rat liver requires the presence of diphosphopyridine nucleotide and cytochrome c. No esterification of inorganic phosphate occurs under these conditions. However, when adenosine triphosphate and Mg++, which have effect on the rate of oxidation, are also present, then inorganic phosphate labeled with P32 is incorporated into an esterified form having the characteristics of the easily hydrolyzable phosphate groups of ATP. This esterification is coupled to the oxidation. Acetoacetate oxidation is excluded as a factor in the esterification, which is therefore coupled only to the DPN-linked oxidation. ADP appears to be the specific phosphate acceptor. The enzymes responsible for the coupled esterification may be selectively inactivated or inhibited by certain compounds without affecting the oxidation itself. No esterification accompanies the interaction of β-hydroxybutyrate with oxalacetate via DPN. The cytochrome system is obligatory for the esterification accompanying BOH oxidation, since its substitution by artificial electron carriers or acceptors causes the esterification reaction to be lost. Experimental attempts to localize the sites of esterification more closely have not given definitive answers. | |abstract=The oxidation of β-hydroxybutyrate to acetoacetate by molecular oxygen in a particulate fraction of rat liver requires the presence of diphosphopyridine nucleotide and cytochrome c. No esterification of inorganic phosphate occurs under these conditions. However, when adenosine triphosphate and Mg++, which have effect on the rate of oxidation, are also present, then inorganic phosphate labeled with P32 is incorporated into an esterified form having the characteristics of the easily hydrolyzable phosphate groups of ATP. This esterification is coupled to the oxidation. Acetoacetate oxidation is excluded as a factor in the esterification, which is therefore coupled only to the DPN-linked oxidation. ADP appears to be the specific phosphate acceptor. The enzymes responsible for the coupled esterification may be selectively inactivated or inhibited by certain compounds without affecting the oxidation itself. No esterification accompanies the interaction of β-hydroxybutyrate with oxalacetate via DPN. The cytochrome system is obligatory for the esterification accompanying BOH oxidation, since its substitution by artificial electron carriers or acceptors causes the esterification reaction to be lost. Experimental attempts to localize the sites of esterification more closely have not given definitive answers. | ||
|keywords= esterification, β-hydroxybutyrate, dihydrodiphosphopyridine nucleotide, oxygen | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Rat | |||
|tissues=Hepatocyte; Liver | |||
|preparations=Isolated Mitochondria | |||
|kinetics=ADP; Pi | |||
|topics=ATP; ADP; AMP; PCr | |||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Revision as of 14:57, 9 June 2012
| Lehninger AL (1949) Esterification of inorganic phosphate coupled to electron transport between dihydrodiphosphopyridine nucleotide and oxygen II. J Biol Chem 178: 625-644. |
Lehninger AL (1949) J Biol Chem
Abstract: The oxidation of β-hydroxybutyrate to acetoacetate by molecular oxygen in a particulate fraction of rat liver requires the presence of diphosphopyridine nucleotide and cytochrome c. No esterification of inorganic phosphate occurs under these conditions. However, when adenosine triphosphate and Mg++, which have effect on the rate of oxidation, are also present, then inorganic phosphate labeled with P32 is incorporated into an esterified form having the characteristics of the easily hydrolyzable phosphate groups of ATP. This esterification is coupled to the oxidation. Acetoacetate oxidation is excluded as a factor in the esterification, which is therefore coupled only to the DPN-linked oxidation. ADP appears to be the specific phosphate acceptor. The enzymes responsible for the coupled esterification may be selectively inactivated or inhibited by certain compounds without affecting the oxidation itself. No esterification accompanies the interaction of β-hydroxybutyrate with oxalacetate via DPN. The cytochrome system is obligatory for the esterification accompanying BOH oxidation, since its substitution by artificial electron carriers or acceptors causes the esterification reaction to be lost. Experimental attempts to localize the sites of esterification more closely have not given definitive answers. • Keywords: esterification, β-hydroxybutyrate, dihydrodiphosphopyridine nucleotide, oxygen
Labels:
Organism: Rat
Tissue;cell: Hepatocyte; Liver"Hepatocyte; Liver" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property.
Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
Regulation: ATP; ADP; AMP; PCr"ATP; ADP; AMP; PCr" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.
Made history
