Evidence in favor of the existence of a kinetic barrier for proton transfer from a surface of bilayer phospholipid membrane to bulk water

Antonenko, Yuri N.; Kovbasnjuk, Olga; Yaguzhinsky, L. S.

doi:10.1016/0005-2736(93)90119-k

Cited by 54 publications

(45 citation statements)

References 20 publications

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“…A key condition for lateral conduction to occur along interfaces is that an energy barrier prevents the free diffusion of protons from the interfacial pathways to the bulk phase (10). The same conclusion was suggested for other systems involving phospholipids (11,12,34). The present study definitively demonstrates that this energy barrier is present with protein layers but is controlled by changes in packing.…”

Section: Biophysics: Gabriel and Teissiésupporting

confidence: 67%

Proton long-range migration along protein monolayers and its consequences on membrane coupling

Gabriel

Teissié

1996

Proc. Natl. Acad. Sci. U.S.A.

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It has been shown with lipid layers and more recently with purple membranes that protons have slow surface-to-bulk transfer. This results in long-range proton lateral conduction along membranes. We report here that such lateral transfer can take place along a pure protein film. It is strongly controlled by the packing. Subtle reorganizations of the protein-protein contact can be biological switches between interfacial and delocalized proton pathways between sources and sinks.

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Section: Biophysics: Gabriel and Teissiésupporting

confidence: 67%

Proton long-range migration along protein monolayers and its consequences on membrane coupling

Gabriel

Teissié

1996

Proc. Natl. Acad. Sci. U.S.A.

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“…In these experiments, ATP synthase was sorbed at the octane-water interface. In this sys tem, ATP synthesis was observed in the presence of ADP and phosphate, and the gradient of a Brønsted acid (pentachlorophenol) at the octane-water inter face was used as a source of energy; the gradient was created by adding pentachlorophenol to the octane phase [6].On the bilayer membrane, we have found the cata lysts that selectively accelerate dissociation of Brøn sted acids [7]. This allowed us to find [8] that a non equilibrium fraction of Brønsted acids with excess free energy was formed on the surface of mitoplasts (mito chondria without the outer membrane), provided that H + pumps function.…”

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confidence: 99%

Brønsted acids bounded to the mitochondrial membranes as a substrate for ATP synthase

Eroshenko

Marakhovskaya

Vangeli

et al. 2012

Dokl Biochem Biophys

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158Starting from 1961, two models for transforma tion of the energy of oxidation reactions in mito chondria have been discussed in the literature. The model of Mitchell [1] implies that the multienzyme phosphorylation system can work in a dissociated form, while the other model (by Williams) considers a supercomplex [2].We have earlier demonstrated that the phosphory lation system is able to function in both modes, corre sponding to two structural states of mitochondria [3]. The operation modes of the phosphorylating system are provided by the system of mitochondrial volume regulation [4,5].In hypotonic media under conditions of low amplitude mitochondrial swelling, the Williams model considers protons (unstably bound to the membrane supercomplex as Brønsted acids) as a substrate for ATP synthase.In 1976, we demonstrated the possibility to use a Brønsted acid as a substrate for ATP synthase using a model system. In these experiments, ATP synthase was sorbed at the octane-water interface. In this sys tem, ATP synthesis was observed in the presence of ADP and phosphate, and the gradient of a Brønsted acid (pentachlorophenol) at the octane-water inter face was used as a source of energy; the gradient was created by adding pentachlorophenol to the octane phase [6].On the bilayer membrane, we have found the cata lysts that selectively accelerate dissociation of Brøn sted acids [7]. This allowed us to find [8] that a non equilibrium fraction of Brønsted acids with excess free energy was formed on the surface of mitoplasts (mito chondria without the outer membrane), provided that H + pumps function.The goal of this work was to prove the formation of Brønsted acids during ATP synthesis on the mito chondrial membranes.A tightly joining of the cristae (Figs. 1 and 2) and, correspondingly, the joining of the outer and inner membranes should be expected. In this process, a two membrane structure of mitoplasts is formed of the outer and inner membranes. Since the outer mem brane is well permeable ("transparent") for hydrogen ions in course of proton pumping, this structure should function as an integral whole interacting with hydrogen ions, possessing excess free energy (accord ing to the scheme in Fig. 1b).We have earlier demonstrated that the measure ment of surface ζ potential (using a Zetasizer Nano ZS device) of mitoplasts can be efficiently used for detecting formation of nonequilibrium Brønsted acids in functional states [8].To selectively accelerate dissociation of mem brane bound Brønsted acids, possessing excess free energy, we increased the concentration of catalyst (HEPES) [7].The measurements were performed in the media with a tonicity of 350 and 120 mOsm. In this experi ment, we compared the measured ζ potential on the surface of functional mitochondria during ATP syn thesis under isotonic and hypotonic conditions. The experiments conducted under hypotonic conditions have demonstrated (Table 1) that the changes in ζ potential on the mitochondrial surface regularly cor relate with the changes in ζ potential on t...

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“…This effect was also observed in other systems [8]. On the planar mem brane, we also registered local H + gradient at the inter phase; formation of this gradient was determined by high kinetic barrier in the reaction of proton release from a surface of lipid bilayer [9]. Recently, we have demonstrat ed formation of local H + gradients in zones of interphas es on the mitochondrial membranes [3] under phospho rylating conditions.…”

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confidence: 61%

“…3 (A 1 * (exp.)). According to the theory [11] and model experiments [9], non penetrating buffer accelerates H + transfer through the interphase. Increase in non penetrating buffer concentration should result in decrease in the external local H + gradient (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The latter may be limited by the stage of proton release from the interphase. This was demonstrated using model system (planar lipid bilayer) [9], non phosphorylating mitochondria [4], and also phosphorylating mitochondrial [3] and submitochondrial particles [5]. Experiments [12] and theoretical calcula tions [11] indicate that low molecular weight buffer should accelerate processes of proton attachment/detachment on polyelectrolytes and, consequently, accelerate reaction of proton detachment from the interphase in the cases when membrane surface includes acid-base groups.…”

Section: Discussionmentioning

confidence: 97%

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Proton transfer through the membrane—water interfaces in uncoupled mitochondria

Yurkov

Fadeeva

Yaguzhinsky

2005

Biochemistry (Moscow)

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Increase in maximal respiration rate of uncoupled mitochondria in response to increase in concentration of non-penetrating buffer has been demonstrated. This phenomenon did not depend on chemical structure of uncouplers and composition of the non-penetrating buffer. Use of covalently attached pH probe, FITC, revealed that at low buffer concentration (3 mM) the H(+)-pump functioning results in local increase in proton concentration on the outer surface of the inner mitochondrial membranes. In other words, local H(+) gradient was generated. Increase in buffer concentration up to 20 mM caused sharp decrease in this gradient, which occurred in parallel to increase in the respiration rate. It is concluded that both effects described here may be attributed to the process of proton transfer through the interfaces of the mitochondrial membrane: the rate of respiratory H(+) pumps of uncoupled mitochondria under conditions of low buffer capacity of medium is limited by the stage of proton release from outer surface of the coupling membrane. The inhibition mechanism of respiration by high concentrations of uncouplers is also discussed.

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Evidence in favor of the existence of a kinetic barrier for proton transfer from a surface of bilayer phospholipid membrane to bulk water

Cited by 54 publications

References 20 publications

Proton long-range migration along protein monolayers and its consequences on membrane coupling

Proton long-range migration along protein monolayers and its consequences on membrane coupling

Brønsted acids bounded to the mitochondrial membranes as a substrate for ATP synthase

Proton transfer through the membrane—water interfaces in uncoupled mitochondria

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