Structure of the K+ complex with nonactin, a macrotetrolide antibiotic possessing highly specific K+ transport properties

Kilbourn, B. T.; Dunitz, Jack D.; Pioda, Lavinia A. R.; Simon, W.

doi:10.1016/0022-2836(67)90370-1

Cited by 223 publications

(72 citation statements)

References 14 publications

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“…Similarly, in the second and third cycles associated with the subsequent additions of CaCl,, Ap appears to go from 245 mV to 232 mV to 247 mV and from 247mV to 233mV to 239mV, while -ZApH goes from 101 mV to I12 mV and 112 mV to 118 mV. [24], in accordance with much other evidence for the K+ ion conducting action of valinomycin in artificial [26-291 (and see [30]) and natural [17,31- (Fig. 6)) it is inconceivable that the unequal distribution of the concentration of I<+ ions across the M phase could be maintained by a metabolically driven K+ ion pump [24].…”

Section: Effect Of Respiration On K+ Distribution Across the K+-perrnsupporting

confidence: 77%

Estimation of Membrane Potential and pH Difference across the Cristae Membrane of Rat Liver Mitochondria

Mitchell

Moyle

1969

European Journal of Biochemistry

571

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The cristae membrane or M phase of resting or respiring rat liver mitochondria becomes relatively permeable to K+ ions in presence of valinomycin. The equilibrium distribution of K+ ions across the membrane can therefore be used to estimate the membrane potential Ay provided that precautions are taken to minimise swelling of the valinomycin-treated mitochondria. The pH difference ApH across the M phase of anaerobic mitochondria has been estimated from the buffering powers of the inner and outer phases and from the change of pH observed on lysing the mitochondria with Triton X-100.

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Section: Effect Of Respiration On K+ Distribution Across the K+-perrnsupporting

confidence: 77%

Estimation of Membrane Potential and pH Difference across the Cristae Membrane of Rat Liver Mitochondria

Mitchell

Moyle

1969

European Journal of Biochemistry

571

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“…Rather than a static pore the antibiotics would form a lipid-soluble complex with the cation, and this passes across a membrane to release the cation on the other side. X-ray-diffraction studies of monensin (Agtarap et al 1967) and nonactin (Kilbourn et al 1967) complexes with cations have shown the cation to be completely surrounded by a hydrophobic 'shell' of antibiotic molecule, in accordance with this proposal. Pressman et al (1967) have shown that valinomycin, dianemycin and nigericin all carried isotopically labelled Rb+ from an aqueous into an organic phase.…”

Section: Methodssupporting

confidence: 65%

“…The above results therefore demonstrate that the antibioticcation complex does not necessarily involve fully hydrated cations. Molecular models of several such types of co-ordination complexes have been discussed by Mueller & Rudin (1967) and by , but the model approach has its limitations: their proposal for the conformation of the actin-cation complex is unlike that deduced by X-ray-diffraction studies (Kilbourn, Dunitz, Pioda & Simon, 1967).…”

Section: Methodsmentioning

confidence: 99%

The action of certain antibiotics on mitochondrial, erythrocyte and artificial phospholipid membranes. The role of induced proton permeability

Henderson

McGivan

Chappell

1969

Biochemical Journal

418

156

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1. The action of the antibiotics enniatin A, valinomycin, the actin homologues, gramicidin, nigericin and dianemycin on mitochondria, erythrocytes and smectic mesophases of lecithin-dicetyl hydrogen phosphate was studied. 2. These antibiotics induced permeability to alkali-metal cations on all three membrane systems. 3. The ion specificity on each membrane system was the same. 4. Enniatin A, valinomycin and the actins did not induce permeability to protons, whereas nigericin and dianemycin rendered all three membrane systems freely permeable to protons. 5. Several differences were noted between permeability induced by nigericin and that induced by gramicidin. 6. The action of all these antibiotics on mitochondrial respiration could be accounted for by changes in passive ion permeability of the mitochondrial membrane similar to those induced in erythrocytes and phospholipid membranes, if it is assumed that a membrane potential is present in respiring mitochondria.The effects of valinomycin on mitochondrial respiration have been investigated extensively

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“…4) was the first large ring ionophore whose conformation was determined. Kilbourn et al [35] found that during complexation, the backbone convoluted into a pattern 'resembling the seam of a tennis ball'. In the K+-nonactin complex, the solvation shell of the K+ ion is entirely replaced by the four oxygen atoms of the tetrahydrofuran ring and the four carbonyl oxygen atoms.…”

Section: Facilitated Ammonium Potassium and Sodium Ion Transfer By mentioning

confidence: 99%

Amperometric detection of the ammonium ion by facilitated ion transfer across the interface between two immiscible electrolyte solutions

Osborne

Girault

1995

Electroanalysis

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Facilitated ion transfer reactions of the ammonium, potassium, and sodium ions with the ionophores dibenzo-18-crown-6, nonactin, and valinomycin were investigated at the water/ 1,2-dichloroethane interface. Association constants for the various reactions studied were calculated to determine the selectivity imparted by the ionophores on the transferring ions. Of the ionophores studied, nonactin was found to be the most selective towards the ammonium ion, with a calculated association constant of 14.1.

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Structure of the K+ complex with nonactin, a macrotetrolide antibiotic possessing highly specific K+ transport properties

Cited by 223 publications

References 14 publications

Estimation of Membrane Potential and pH Difference across the Cristae Membrane of Rat Liver Mitochondria

Estimation of Membrane Potential and pH Difference across the Cristae Membrane of Rat Liver Mitochondria

The action of certain antibiotics on mitochondrial, erythrocyte and artificial phospholipid membranes. The role of induced proton permeability

Amperometric detection of the ammonium ion by facilitated ion transfer across the interface between two immiscible electrolyte solutions

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