Chance 1955 J Biol Chem-III: Difference between revisions
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Revision as of 12:32, 18 December 2013
Chance B, Williams GR (1955) Respiratory enzymes in oxidative phosphorylation: III. The steady state. J Biol Chem 217: 409-427. |
Chance B, Williams GR (1955) J Biol Chem
Abstract: In a complex enzymatic sequence the site of action of substrates and inhibitors is clearly marked by the way they affect the steady state concentrations of the components of the system. Antimycin A, for example, inhibits respiration in the succinic oxidase system and at the same time increases the steady state reduction of cytochrome b and decreases that of cytochromes c, a, and aa3. In the oxidative phosphorylation system of liver mitochondria, phosphate and phosphate acceptors cause a considerable activation of respiration and may do so by a reversal of inhibitory reactions along the respiratory chain. Thus measurements of changes in the steady state of the members of the respiratory chain upon initiation and cessation of oxidative phosphorylation of ADP may identify sites in the chain where the phosphorylation reactions occur. โข Keywords: Respiratory enzymes, Respiratory chain, Steady state, OXPHOS, Liver mitochondria
Labels: MiParea: Respiration
Organism: Rat, Guinea pig
Tissue;cell: Liver
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.
Coupling state: LEAK, OXPHOS
Made history