Chance 1961 J Biol Chem-III: Difference between revisions
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{{Publication | {{Publication | ||
|title=Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria III. Substrate requirements for pyridine nucleotide reduction in mitochondria. J Biol Chem 236: 1555- | |title=Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria III. Substrate requirements for pyridine nucleotide reduction in mitochondria. J Biol Chem 236:1555-61. | ||
|info=[http://www. | |info=[http://www.ncbi.nlm.nih.gov/pubmed/13692278 PMID: 13692278 Open Access] | ||
|authors=Chance B, Hollunger G | |authors=Chance B, Hollunger G | ||
|year=1961 | |year=1961 | ||
|journal=J Biol Chem | |journal=J Biol Chem | ||
|abstract= | |abstract=# A specific succinate requirement for energy-linked reduction of mitochondrial pyridine nucleotide is demonstrated in pigeon heart and guinea pig kidney mitochondria. | ||
# A | # The succinate used in this reduction can be generated in the oxidation of malate plus glutamate or of Ξ±-ketoglutarate. Β | ||
# The | # The role of succinate is identified by the specific inhibitory responses of the reaction to malonate, phosphate, and fumarate. Β | ||
# The | # At least two kinds of mitochondrial pyridine nucleotide are shown to be reducible in State 4: (a) about one-third in the absence of added succinate in a malonate-insensitive reaction in the presence of a substrate such as malate plus glutamate and (b) about two-thirds in the presence of added succinate in a malonate-sensitive, energy-linked reaction.Β These two kinds of pyridine nucleotide may be considered to be compartmented. | ||
# At | |keywords=Pyridine nucleotide, Succinate | ||
}} | |||
== Made history == | |||
::::* [[Mitochondria and bioblasts: Made history]] | |||
{{Labeling | {{Labeling | ||
|organism= | |organism=Guinea pig, Birds | ||
|tissues= | |tissues=Heart, Kidney | ||
|preparations=Isolated | |preparations=Isolated mitochondria | ||
|enzymes=Complex II; | |enzymes=Complex II;succinate dehydrogenase | ||
|topics= | |topics=Substrate | ||
|couplingstates=OXPHOS | |||
|additional=Made history | |additional=Made history | ||
}} | }} |
Latest revision as of 10:45, 6 July 2022
Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria III. Substrate requirements for pyridine nucleotide reduction in mitochondria. J Biol Chem 236:1555-61. |
Chance B, Hollunger G (1961) J Biol Chem
Abstract:
- A specific succinate requirement for energy-linked reduction of mitochondrial pyridine nucleotide is demonstrated in pigeon heart and guinea pig kidney mitochondria.
- The succinate used in this reduction can be generated in the oxidation of malate plus glutamate or of Ξ±-ketoglutarate.
- The role of succinate is identified by the specific inhibitory responses of the reaction to malonate, phosphate, and fumarate.
- At least two kinds of mitochondrial pyridine nucleotide are shown to be reducible in State 4: (a) about one-third in the absence of added succinate in a malonate-insensitive reaction in the presence of a substrate such as malate plus glutamate and (b) about two-thirds in the presence of added succinate in a malonate-sensitive, energy-linked reaction. These two kinds of pyridine nucleotide may be considered to be compartmented.
β’ Keywords: Pyridine nucleotide, Succinate
Made history
Labels:
Organism: Guinea pig, Birds
Tissue;cell: Heart, Kidney
Preparation: Isolated mitochondria
Enzyme: Complex II;succinate dehydrogenase
Regulation: Substrate
Coupling state: OXPHOS
Made history