Protons @ interfaces: Implications for biological energy conversion

Mulkidjanian AY, Heberle J, Cherepanov DA (2006)
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1757(8): 913-930.

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The review focuses on the anisotropy of proton transfer at the surface of biological membranes. We consider (i) the data from "pulsed" experiments, where light-triggered enzymes capture or eject protons at the membrane surface, (ii) the electrostatic properties of water at charged interfaces, and (iii) the specific structural attributes of proton-translocating enzymes. The pulsed experiments revealed that proton exchange between the membrane surface and the bulk aqueous phase takes as much as about I ms, but could be accelerated by added mobile pH-buffers. Since the accelerating capacity of the latter decreased with the increase in their electric charge, it was concluded that the membrane surface is separated from the bulk aqueous phase by a barrier of electrostatic nature. The barrier could arise owing to the water polarization at the negatively charged membrane surface. The barrier height depends linearly on the charge of penetrating ions; for protons, it has been estimated as about 0.12 eV. While the proton exchange between the surface and the bulk aqueous phase is retarded by the interfacial barrier, the proton diffusion along the membrane, between neighboring enzymes, takes only microseconds. The proton spreading over the membrane is facilitated by the hydrogen-bonded networks at the surface. The membrane-buried layers of these networks can eventually serve as a storage/buffer for protons (proton sponges). As the proton equilibration between the surface and the bulk aqueous phase is slower than the lateral proton diffusion between the "sources" and "sinks", the proton activity at the membrane surface, as sensed by the energy transducing enzymes at steady state, might deviate from that measured in the adjoining water phase. This trait should increase the driving force for ATP synthesis, especially in the case of alkaliphilic bacteria. (c) 2006 Elsevier B.V. All rights reserved.
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Mulkidjanian AY, Heberle J, Cherepanov DA. Protons @ interfaces: Implications for biological energy conversion. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS. 2006;1757(8):913-930.
Mulkidjanian, A. Y., Heberle, J., & Cherepanov, D. A. (2006). Protons @ interfaces: Implications for biological energy conversion. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1757(8), 913-930. doi:10.1016/j.bbabio.2006.02.015
Mulkidjanian, A. Y., Heberle, J., and Cherepanov, D. A. (2006). Protons @ interfaces: Implications for biological energy conversion. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1757, 913-930.
Mulkidjanian, A.Y., Heberle, J., & Cherepanov, D.A., 2006. Protons @ interfaces: Implications for biological energy conversion. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1757(8), p 913-930.
A.Y. Mulkidjanian, J. Heberle, and D.A. Cherepanov, “Protons @ interfaces: Implications for biological energy conversion”, BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, vol. 1757, 2006, pp. 913-930.
Mulkidjanian, A.Y., Heberle, J., Cherepanov, D.A.: Protons @ interfaces: Implications for biological energy conversion. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS. 1757, 913-930 (2006).
Mulkidjanian, Armen Y., Heberle, Joachim, and Cherepanov, Dmitry A. “Protons @ interfaces: Implications for biological energy conversion”. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1757.8 (2006): 913-930.
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PMID: 21419607
Proton diffusion along biological membranes.
Medvedev ES, Stuchebrukhov AA., J Phys Condens Matter 23(23), 2011
PMID: 21613715
Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that support the ability to grow in an external pH range from 7.5 to 11.4.
Janto B, Ahmed A, Ito M, Liu J, Hicks DB, Pagni S, Fackelmayer OJ, Smith TA, Earl J, Elbourne LD, Hassan K, Paulsen IT, Kolstø AB, Tourasse NJ, Ehrlich GD, Boissy R, Ivey DM, Li G, Xue Y, Ma Y, Hu FZ, Krulwich TA., Environ Microbiol 13(12), 2011
PMID: 21951522
Effect of the alkaline cations on the stability of the model polynucleotide poly(dG-dC)·poly(dG-dC).
Airoldi M, Gennaro G, Giomini M, Giuliani AM, Giustini M., J Biomol Struct Dyn 29(3), 2011
PMID: 22066543
F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.
Hicks DB, Liu J, Fujisawa M, Krulwich TA., Biochim Biophys Acta 1797(8), 2010
PMID: 20193659
The obligate alkaliphile Bacillus clarkii K24-1U retains extruded protons at the beginning of respiration.
Yoshimune K, Morimoto H, Hirano Y, Sakamoto J, Matsuyama H, Yumoto I., J Bioenerg Biomembr 42(2), 2010
PMID: 20306123
Functional interactions between membrane-bound transporters and membranes.
Ojemyr LN, Lee HJ, Gennis RB, Brzezinski P., Proc Natl Acad Sci U S A 107(36), 2010
PMID: 20798065
A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential.
Ogami S, Hijikata S, Tsukahara T, Mie Y, Matsuno T, Morita N, Hara I, Yamazaki K, Inoue N, Yokota A, Hoshino T, Yoshimune K, Yumoto I., Extremophiles 13(3), 2009
PMID: 19266156
Co-evolution of primordial membranes and membrane proteins.
Mulkidjanian AY, Galperin MY, Koonin EV., Trends Biochem Sci 34(4), 2009
PMID: 19303305
Recent advances in structure-functional studies of mitochondrial factor B.
Belogrudov GI., J Bioenerg Biomembr 41(2), 2009
PMID: 19377834
pH Modulation of efflux pump activity of multi-drug resistant Escherichia coli: protection during its passage and eventual colonization of the colon.
Martins A, Spengler G, Rodrigues L, Viveiros M, Ramos J, Martins M, Couto I, Fanning S, Pagès JM, Bolla JM, Molnar J, Amaral L., PLoS One 4(8), 2009
PMID: 19684858
An AcrAB-mediated multidrug-resistant phenotype is maintained following restoration of wild-type activities by efflux pump genes and their regulators.
Martins A, Iversen C, Rodrigues L, Spengler G, Ramos J, Kern WV, Couto I, Viveiros M, Fanning S, Pages JM, Amaral L., Int J Antimicrob Agents 34(6), 2009
PMID: 19734019
Dielectric relaxation dynamics of water in model membranes probed by terahertz spectroscopy.
Tielrooij KJ, Paparo D, Piatkowski L, Bakker HJ, Bonn M., Biophys J 97(9), 2009
PMID: 19883591
The past and present of sodium energetics: may the sodium-motive force be with you.
Mulkidjanian AY, Dibrov P, Galperin MY., Biochim Biophys Acta 1777(7-8), 2008
PMID: 18485887
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Mulkidjanian AY, Cherepanov DA., Photochem Photobiol Sci 5(6), 2006
PMID: 16761086
Localized proton microcircuits at the biological membrane-water interface.
Brändén M, Sandén T, Brzezinski P, Widengren J., Proc Natl Acad Sci U S A 103(52), 2006
PMID: 17172452

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