Cytochrome C‐nucleotide Complexes and the Role of Unpaired Electrons in Coupling Processes

Kayushin, L.P.; Ajipa, Yaroslav I.

doi:10.1111/j.1749-6632.1973.tb15267.x

Cited by 10 publications

(4 citation statements)

References 9 publications

(1 reference statement)

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“…Using n.m.r. spectroscopy Kayushin & Ajipa (1973) found that the nucleoside moiety as well as the phosphates of ATP interact with cytochrome c. Our data indicate that the presence of a triphosphate tail is the prime determinant of the high-affinity binding, but that some contribution is made by the nucleoside moiety.…”

Section: Characteristics Of the Binding Sitementioning

confidence: 54%

“…Studies involving gel filtration (Margalit & Schejter, 1973;, electrophoresis (Margoliash et al, 1970), ion-exchange chromatography (Brautigan et al, 1978), n.m.r. spectroscopy (Kayushin & Ajipa, 1973;Stellwagen & Schulman, 1973;Andersson et al, 1979;Feng & Englander, 1990) and chemical modification (Taborsky & McCollum, 1979;Corthesy & Wallace, 1988) have shown that cytochrome c is capable of specific binding of certain anions, particularly phosphate. found that oxidized and reduced horse cytochrome c bind an average of 2.47 and 1.64 molecules of ATP per molecule of protein respectively at an ATP concentration of 1 mm in 5 mM-Tris/cacodylate buffer.…”

Section: Introductionmentioning

confidence: 99%

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The specificity and Kd at physiological ionic strength of an ATP-binding site on cytochrome c suit it to a regulatory role

Craig

Wallace

1991

Biochemical Journal

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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 function of the degree of phosphorylation of the nucleotide, than of the nature of the nucleoside moiety. Thus under physiological conditions the degree of occupancy of this site is proportional to the energy state of the cell, providing a means for the regulation of the respiratory chain which is sensitive to cytoplasmic ATP levels.

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Section: Characteristics Of the Binding Sitementioning

confidence: 54%

Section: Introductionmentioning

confidence: 99%

The specificity and Kd at physiological ionic strength of an ATP-binding site on cytochrome c suit it to a regulatory role

Craig

Wallace

1991

Biochemical Journal

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“…A complicating problem in most of these studies is that no distinction was made between the interaction of nucleotides with cytochrome c oxidase or with its substrate, cytochrome c (Ferguson-Miller et al, 1976;Roberts & Hess, 1977;Osheroff etal., 1978;Huther & Kadenbach, 1986;Malatesta et al, 1987;Bisson et al, 1987;Rigoulet et al, 1987;Reimann et al, 1988;Antonini et al, 1988). Specific binding sites for adenine nucleotides have been identified on cytochrome c (Margoliash et al" 1970;Stellwagen & Shulman, 1973; Margalit & Schejter, 1973;Kayushin & Ajipa, 1973;Corthesy & Wallace, 1986. The binding of ATP to cytochrome c, at millimolar concentrations of ATP, diminishes the electron flow in the respiratory chain (Craig & Wallace, 1991, thus mimicking claimed effects of adenine nucleotides on the kinetics of cytochrome c oxidase.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Cytochrome c Oxidase by Interaction of ATP at Two Binding Sites, One on Subunit VIa

Taanman¹,

Turina²,

Capaldi³

1994

Biochemistry

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Cytochrome c oxidase isolated from a wild-type yeast strain and a mutant in which the gene for subunit VIa had been disrupted were used to study the interaction of adenine nucleotides with the enzyme complex. At low ionic strength (25 mM potassium phosphate), in the absence of nucleotides, the cytochrome c oxidase activity of the mutant enzyme lacking subunit VIa was higher than that of the wild-type enzyme. Increasing concentrations of ATP, in the physiological range, enhanced the cytochrome c oxidase activity of the mutant much more than the activity of the wild-type strain, whereas ADP, in the same concentration range, had no significant effect on the activity of the cytochrome c oxidase of either strain. These results indicate an interaction of ATP with subunit VIa in the wild-type enzyme that prevents the stimulation of the activity observed in the mutant enzyme. The stimulation of the mutant enzyme implies the presence of a second ATP binding site on the enzyme. Quantitative titrations with the fluorescent adenine nucleotide analogues 2'(or 3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate (TNP-ATP) and 2'(or 3')-O-(2,4,6-trinitrophenyl)adenosine 5'-diphosphate (TNP-ADP) confirmed the presence of two binding sites for adenine nucleotides per monomer of wild-type cytochrome c oxidase and one binding site per monomer of mutant enzyme. Covalent photolabeling of yeast cytochrome c oxidase with radioactive 2-azido-ATP further confirmed the presence of an ATP binding site on subunit VIa.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…Studies employing gel filtration (Margalit & Schejter, 1973), electrophoresis (Margoliash et al, 1970), ionexchange chromatography (Brautigan et al, 1978) and n.m.r. spectroscopy (Kayushin & Ajipa, 1973) have shown that cytochrome c binds, in a specific manner, certain anions. If this binding were to modulate the interaction of the protein with the other redox carriers, then there would exist the basis for a system whereby the relative concentrations of such anions could have a controlling influence on cellular redox processes.…”

Section: Introductionmentioning

confidence: 99%

The oxidation-state-dependent ATP-binding site of cytochrome c. A possible physiological significance

Corthésy¹,

Wallace²

1986

Biochemical Journal

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Cytochrome c binds certain physiological anions that are known to modulate the biological properties of the protein, although it is not known whether this effect is fortuitous or has physiological significance. We have examined the ability of the protein and its semisynthetic analogues to associate with certain of these anions, e.g. ATP, ADP, Pi and citrate. Our results show that specific residues or clusters of residues on the surface of horse heart cytochrome c are involved in the recognition sites for these anions. We also observed that binding at one site is linked to the oxidation state of the protein.

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Cytochrome C‐nucleotide Complexes and the Role of Unpaired Electrons in Coupling Processes

Cited by 10 publications

References 9 publications

The specificity and Kd at physiological ionic strength of an ATP-binding site on cytochrome c suit it to a regulatory role

The specificity and Kd at physiological ionic strength of an ATP-binding site on cytochrome c suit it to a regulatory role

Regulation of Cytochrome c Oxidase by Interaction of ATP at Two Binding Sites, One on Subunit VIa

The oxidation-state-dependent ATP-binding site of cytochrome c. A possible physiological significance

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