1995
DOI: 10.1021/bi00008a036 View full text |Buy / Rent full text
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Abstract: We have proposed that the binding of ATP at a site of substantial affinity and specificity could regulate the activity of cytochrome c with its physiological partners and thus the overall efficiency of mitochondrial electron transport. We now describe the use of ATP affinity-labeled protein to test the effect of occupancy of that site, which includes the invariant arginine 91, on the activity of cytochrome c with purified cytochrome c reductase and oxidase and its association with the mitochondrial inner membr… Show more

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“…Secondly, the substrate pressure in the respiratory chain, and thus the ferro/ferricytochrome c ratio, affects mitochondrial respiration. This substrate control is further modulated by anions, in particular by the concentrations of ADP and ATP, which also bind to cytochrome c (Corthesy and Wallace, 1986) and modulate the rate of electron transfer from ferrocytochrome c to cytochrome-c oxidase (Craig and Wallace, 1995). Thirdly, the concentration of oxygen affects mitochondrial respiration, and fourthly, the matrix ATP/ADP ratio, as described in the present paper, results in allosteric feedback inhibition.…”
Section: Discussionmentioning
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“…Secondly, the substrate pressure in the respiratory chain, and thus the ferro/ferricytochrome c ratio, affects mitochondrial respiration. This substrate control is further modulated by anions, in particular by the concentrations of ADP and ATP, which also bind to cytochrome c (Corthesy and Wallace, 1986) and modulate the rate of electron transfer from ferrocytochrome c to cytochrome-c oxidase (Craig and Wallace, 1995). Thirdly, the concentration of oxygen affects mitochondrial respiration, and fourthly, the matrix ATP/ADP ratio, as described in the present paper, results in allosteric feedback inhibition.…”
Section: Discussionmentioning
“…S5) and residual peroxidase activity (Fig. 4B) (26) and its ability to relocate into the cytosol during apoptosis (3). The mitochondrial phospholipid CL binds tightly to cyt c and is particularly effective in unfolding the protein (4).…”
Section: Resultsmentioning
“…Studies of the effect of anions on the activity of isolated COX suggested nonspeci c ionic effects, because the interaction between cytochrome c and COX is of electrostatic nature (19,(30)(31)(32). However, speci c binding sites for ATP and ADP have been identi ed on cytochrome c, which in turn may decrease the electron transfer from cytochrome c to the oxidase (33)(34)(35).…”
Section: Interaction Of Adenylic Nucleotides On Coxmentioning