Chance 1955 J Biol Chem-III

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Chance B, Williams GR (1955) Respiratory enzymes in oxidative phosphorylation: III. The steady state. J Biol Chem 217:409-27.

» PMID: 13271404 Open Access

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.

Keywords: Respiratory enzymes, Respiratory chain, Steady state, OXPHOS, Liver mitochondria


Labels: MiParea: Respiration 


Organism: Rat, Guinea pig  Tissue;cell: Liver  Preparation: Isolated mitochondria 


Coupling state: LEAK, OXPHOS  Pathway: N, S 


Made history 

Definition of States 1 to 5

Made history