330 - Determination of surface charge of bilayer lipid membranes

Cherny, Vladimir V.; Sokolov, V.S.; Abidor, I.G.

doi:10.1016/0302-4598(80)80002-x

Cited by 35 publications

(8 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The effect of electrical field on membrane deformation was observed, in part, by the method of inner field compensation on the bilayer membranes. Its application showed a change in the membrane thickness and capacitance when the membrane interacts with various compounds [ 85 , 86 , 87 ], including the membrane-bound proton fraction [ 3 , 4 ]. We proposed that a similar effect may also present in the MIM under proton pump functioning [ 2 ].…”

Section: Discussionmentioning

confidence: 99%

Contribution of the Collective Excitations to the Coupled Proton and Energy Transport along Mitochondrial Cristae Membrane in Oxidative Phosphorylation System

Nesterov

Yaguzhinsky²,

Василов³

et al. 2022

Entropy

View full text Add to dashboard Cite

The results of many experimental and theoretical works indicate that after transport of protons across the mitochondrial inner membrane (MIM) in the oxidative phosphorylation (OXPHOS) system, they are retained on the membrane–water interface in nonequilibrium state with free energy excess due to low proton surface-to-bulk release. This well-established phenomenon suggests that proton trapping on the membrane interface ensures vectorial lateral transport of protons from proton pumps to ATP synthases (proton acceptors). Despite the key role of the proton transport in bioenergetics, the molecular mechanism of proton transfer in the OXPHOS system is not yet completely established. Here, we developed a dynamics model of long-range transport of energized protons along the MIM accompanied by collective excitation of localized waves propagating on the membrane surface. Our model is based on the new data on the macromolecular organization of the OXPHOS system showing the well-ordered structure of respirasomes and ATP synthases on the cristae membrane folds. We developed a two-component dynamics model of the proton transport considering two coupled subsystems: the ordered hydrogen bond (HB) chain of water molecules and lipid headgroups of MIM. We analytically obtained a two-component soliton solution in this model, which describes the motion of the proton kink, corresponding to successive proton hops in the HB chain, and coherent motion of a compression soliton in the chain of lipid headgroups. The local deformation in a soliton range facilitates proton jumps due to water molecules approaching each other in the HB chain. We suggested that the proton-conducting structures formed along the cristae membrane surface promote direct lateral proton transfer in the OXPHOS system. Collective excitations at the water–membrane interface in a form of two-component soliton ensure the coupled non-dissipative transport of charge carriers and elastic energy of MIM deformation to ATP synthases that may be utilized in ATP synthesis providing maximal efficiency in mitochondrial bioenergetics.

show abstract

Section: Discussionmentioning

confidence: 99%

Contribution of the Collective Excitations to the Coupled Proton and Energy Transport along Mitochondrial Cristae Membrane in Oxidative Phosphorylation System

Nesterov

Yaguzhinsky²,

Василов³

et al. 2022

Entropy

View full text Add to dashboard Cite

show abstract

“…Its application showed a change of the membrane thickness and capacitance when the membrane interacts with various compounds (Abidor I.G. et al 1980; Cherny et al 1980; Jiménez-Munguía et al 2019), including the membrane-bound proton fraction (Antonenko et al 1993; Tashkin et al 2019). We proposed that a similar effect may also present in the MIM under proton pump functioning (Nesterov et al 2022).…”

Section: Discussionmentioning

confidence: 99%

Contribution of the collective excitations to the coupled proton and energy transport along mitochondrial crista membrane in oxidative phosphorylation system

Nesterov

Yaguzhinskiy

Василов

et al. 2022

Preprint

View full text Add to dashboard Cite

The results of many experimental and theoretical works indicate that after transport of protons across the mitochondrial inner membrane (MIM) in oxidative phosphorylation system (OXPHOS), they are retained on the membrane-water interface in non-equilibrium state with free energy excess due to low proton surface-to-bulk release. This well-established phenomenon suggests that proton trapping on the membrane interface ensures vectorial lateral transport of protons from proton pumps to ATP synthases (proton acceptors). Despite the key role of the proton transport in bioenergetics, the molecular mechanism of proton transfer in OXPHOS is not yet completely established. Here, we developed a dynamic model of long-range transport of energized protons along the MIM accompanied by collective excitation of localized wave prorogating on the membrane surface. Our model is based on the new data on the macromolecular organization of OXPHOS showing the well-ordered structure of respirasomes and ATP synthases on the cristae membrane folds. We developed a two-component dynamic model of the proton transport considering two coupled subsystems: the ordered hydrogen bond chain of water molecules and lipid headgroups of MIM. We analytically obtained two-component soliton solution in this model, which describe the motion of the proton kink, corresponding to successive proton hops in the HB chain, and coherent motion of a compression soliton in the chain of lipid headpolar groups. The local deformation in a soliton range facilitates proton jumps due to water molecules approaching each other in the HB chain. We suggested that the proton-conducting structures formed along the cristae membrane surface promotes direct lateral proton transfer in OXPHOS. Collective excitations at the water-membrane interface in a form of two-component soliton ensure the coupled non-dissipative transport of charge carriers and elastic energy of MIM deformation to ATP synthases that may be utilized in ATP synthesis providing maximal efficiency in mitochondrial bioenergetics.

show abstract

“…The measurement method of the surface potential exploits the nonmonotonic voltage dependence of membrane capacitance [ 28 , 29 , 30 ]. In [ 29 ], it was shown that the voltage corresponding to the minimum of the capacitance current could be uniquely calculated using current responses to upward and downward half-periods of the triangular voltage.…”

Section: Methodsmentioning

confidence: 99%

Effect of Cytochrome C on the Conductance of Asolectin Membranes and the Occurrence of Through Pores at Different pHs

et al. 2023

View full text Add to dashboard Cite

The study of the electrical parameters of asolectin bilayer lipid membranes in the presence of cytochrome c (cyt c) at various concentrations showed that an increase in the concentration of cyt c leads to an increase in the membrane conductance and the appearance of through pores. The studied membranes did not contain cardiolipin, which is commonly used in studying the effect of cyt c on membrane permeability. In the presence of cyt c, discrete current fluctuations were recorded. The occurrence of these fluctuations may be associated with the formation of through pores. The diameter of these pores was ~0.8 nm, which is smaller than the size of the cyt c globule (~3 nm). Measurements carried out at pH values from 6.4 to 8.4 showed that the concentration dependence of the membrane conductance increases with increasing pH. To assess the binding of cyt c to the bilayer, we measured the concentration and pH dependences of the difference in surface potentials induced by the unilateral addition of cyt c. The amount of bound cyt c at the same concentrations decreased with increasing pH, which did not correspond to the conductance trend. An analysis of conductance traces leads to the conclusion that an increase in the integral conductance of membranes is associated with an increase in the lifetime of pores. The formation of “long-lived” pores, of which the residence time in the open state is longer than in the closed state, was achieved at various combinations of pHs and cyt c concentrations: the higher the pH, the lower the concentration at which the long-lived pores appeared and, accordingly, a higher conductance was observed. The increase in conductance and the formation of transmembrane pores are not due to the electrostatic interaction between cyt c and the membrane. We hypothesize that an increase in pH leads to a weakening of hydrogen bonds between lipid heads, which allows cyt c molecules to penetrate into the membrane. This disrupts the order of the bilayer and leads to the occurrence of through pores.

show abstract

330 - Determination of surface charge of bilayer lipid membranes

Cited by 35 publications

References 6 publications

Contribution of the Collective Excitations to the Coupled Proton and Energy Transport along Mitochondrial Cristae Membrane in Oxidative Phosphorylation System

Contribution of the Collective Excitations to the Coupled Proton and Energy Transport along Mitochondrial Cristae Membrane in Oxidative Phosphorylation System

Contribution of the collective excitations to the coupled proton and energy transport along mitochondrial crista membrane in oxidative phosphorylation system

Effect of Cytochrome C on the Conductance of Asolectin Membranes and the Occurrence of Through Pores at Different pHs

Contact Info

Product

Resources

About