Protons @ interfaces: Implications for biological energy conversion

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

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Abstract / Bemerkung
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.
Stichworte
alkaliphilic bacteria; chemiosmotic coupling; membrane potential; proton transfer; ATP synthesis; nonlocal electrostatics; surface potential; Grotthus mechanism
Erscheinungsjahr
2006
Zeitschriftentitel
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Band
1757
Ausgabe
8
Seite(n)
913-930
ISSN
0005-2728
Page URI
https://pub.uni-bielefeld.de/record/1597360

Zitieren

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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