1991
DOI: 10.1042/bj2790781
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Abstract: Cytochrome c binds ATP with marked specificity at a site that contains the evolutionarily invariant residue Arg-91. The binding of ATP to this site was studied using equilibrium gel filtration, equilibrium dialysis and affinity chromatography. At physiological ionic strength the affinity is such that the major change in occupancy coincides with the normal cellular ATP concentration range, and the degree of saturation is proportional to the ratio of [ATP]/[ADP]. The specificity of binding at this site is more a… Show more

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Cited by 30 publications
(42 citation statements)
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“…A high affinity binding site for ATP has been described and shown to involve the invariant Arg 91 (5,(7)(8)(9)(10). The involvement of Arg 91 in binding of ATP and consequent modulation of electron transfer by the protein has been investigated previously by semisynthetic analogs of cyt c in which this single arginine residue of the 66 -104 peptide was chemically modified by cyclohexane-1,2-dione prior to ligation with the 1-65 peptide (10).…”
Section: Discussionmentioning
confidence: 99%
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“…A high affinity binding site for ATP has been described and shown to involve the invariant Arg 91 (5,(7)(8)(9)(10). The involvement of Arg 91 in binding of ATP and consequent modulation of electron transfer by the protein has been investigated previously by semisynthetic analogs of cyt c in which this single arginine residue of the 66 -104 peptide was chemically modified by cyclohexane-1,2-dione prior to ligation with the 1-65 peptide (10).…”
Section: Discussionmentioning
confidence: 99%
“…First, elution times on an ATP-agarose column equilibrated in 35 mM phosphate were measured. The observed retention times in this column vary widely for different cyt c analogs and provide a measure of the affinity of the protein for ATP (7). This method revealed [Nle 91 ]cyt c to bind ATP substantially less effectively than the native protein, and the elution time from a column with immobilized ATP is half that of cyt c (12 versus 24 min).…”
mentioning
confidence: 98%
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“…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
confidence: 99%