Field-dependent Mechanism of Anomalous Proton Conductivity and the Polarizability of Hydrogen Bonds with Tunneling Protons

Weidemann, E. G.; Zuńdel, Georg

doi:10.1515/zna-1970-0509

Cited by 114 publications

(30 citation statements)

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“…Contribution of the π‐conjugated phenyl moieties of the peptide to the observed polarizability was found to be small by the significantly lower signal of Aβ‐Q. Indeed, it was reported that proton polarizability through hydrogen bonds network is two orders of magnitude higher than electron polarizability . Hence, we assign the EFM signal to mobile proton charges in the peptide fibrils.…”

Section: Resultsmentioning

confidence: 75%

Significant Enhancement of Proton Transport in Bioinspired Peptide Fibrils by Single Acidic or Basic Amino Acid Mutation

Silberbush

Amit

Roy

et al. 2017

Adv Funct Materials

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Bioinspired materials are extremely suitable for the development of biocompatible and environmentally friendly functional materials. Peptide‐based assemblies are remarkably attractive for such tasks, since they provide a simple way to fuse together functional and structural protein motifs in artificial materials. Motivated by this idea, it is shown here that the introduction of a single acidic, or basic, amino acid into the side chain of a heptameric self‐assembling peptide increases proton conduction in the resulting fibers by two orders of magnitude. This self‐doping effect is much more pronounced than the effect induced by the peptide's acidic and basic termini groups. Furthermore, the self‐doping process is found to be significantly more effective for acidic side chains than for basic ones due to both much more effective self‐doping process, resulting in an order of magnitude larger concentration of charge carriers for the acidic assemblies, and higher mobility of the formed charge carriers – almost threefolds in this case. This work facilitates the realization of unique bioinspired self‐assembled proton conducting materials that may find uses in the emerging bioprotonic technology. The presented design flexibility and, in particular, the ability to introduce both proton and proton holes further extend the usefulness of these materials.

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Section: Resultsmentioning

confidence: 75%

Significant Enhancement of Proton Transport in Bioinspired Peptide Fibrils by Single Acidic or Basic Amino Acid Mutation

Silberbush

Amit

Roy

et al. 2017

Adv Funct Materials

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“…The aim of the present article is to show that trigonometric DWP provides the expressions for the energy levels and their corresponding wave functions for HB in CrOOH and KH 2 PO 4 along with their polarizability. The tunneling process for a proton is known to yield a dominant contribution to the extremely high polarizability of HB [22], [23], [24], [25], [26]. This problem was thoroughly investigated by Zundel and co-authors (see [22], [25], [26] and refs.…”

Section: Introductionmentioning

confidence: 99%

Analytic treatment of IR-spectroscopy data for double well potential

Sitnitsky

2019

Computational and Theoretical Chemistry

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A theoretical scheme for the analysis of experimental data on IR spectroscopy for a quantum particle in a double well potential (DWP) is suggested. The analysis is based on the trigonometric DWP for which the exact analytic solution of the Schrödinger equation is available. The corresponding energy levels along with their wave functions are expressed via special functions implemented in Mathematica (spheroidal function and its spectrum of eigenvalues). As a result trigonometric DWP makes the calculation of the energy levels an extremely easy procedure. It contains three parameters allowing one to model the most important characteristics of DWP (barrier height and the distance between the minima of the potential) along with the required asymmetry. Our approach provides an accurate calculation of the energy spectrum for hydrogen bonds in chromous acid (CrOOH) and potassium dihydrogen phosphate (KH 2 PO 4 ) along with their polarizability in agreement with available experimental data.

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“…These proton polarizabilities arise because of shifts of the protons within these hydrogen bonds. All of these results were obtained by theoretical treatments (Weidemann and Zundel, 1970;Janoschek et al, 1973;Zundel, 1976;Eckert and Zundel, 1987; Borgis et al, 1992; Zundel and Eckert, 1989) based on and proven by a very large number of infrared (Zundel (1976), Zundel (1992a), and references therein) and Raman Danninger and Zundel (1980) studies. These proton polarizabilities are particularly large in the case of hydrogen-bonded chains because in such chains a collective proton-tunneling occurs (Zundel, 1976;Eckert and Zundel, 1988a, b;Zundel, 1992b;Zundel and Brzezinski, 1992).…”

Section: Introductionmentioning

confidence: 88%

The F0 complex of the ATP synthase of Escherichia coli contains a proton pathway with large proton polarizability caused by collective proton fluctuation

Bartl¹,

Deckers-Hebestreit²,

Altendorf³

et al. 1995

Biophysical Journal

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The F0 complex of the Escherichia coli ATP synthase embedded into cardiolipin liposomes was studied by FT-IR spectroscopy. For comparison, respective studies were performed with dried F0 liposomes and with F0 liposomes treated with N,N'-dicyclohexyl-carbodiimide (DCCD), which binds to Asp-61 of subunit c. Furthermore, the effect of H2O-->D2O exchange on the infrared spectrum was investigated. With F0 liposomes an infrared continuum is observed beginning at about 3000 cm-1 and extending toward smaller wavenumbers. In the DCCD-treated sample, this continuum is no longer observed. It vanishes also with drying of the liposomes. After H2O-->D2O exchange, this infrared continuum begins at about 2350 cm-1 and is less intense. All of these results demonstrate that a proton pathway in native F0 is present, in which the protons are shifted in a hydrogen-bonded chain with large proton polarizability due to collective proton tunneling. With the D2O-hydrated system, deuteron polarizability due to collective deuteron motion is observed, but the polarizability due to collective deuteron motion is smaller. Such pathways are very efficient, because they conduct protons or deuterons within picoseconds. These pathways lose their polarizability if the F0 complex is blocked by DCCD or if the liposomes are dried. On the basis of our results on the proton polarizability of hydrogen bonds and hydrogen-bonded systems and on the basis of structural data from the literature, the nature of the proton pathway of the F0 complex of E. coli is discussed.

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Field-dependent Mechanism of Anomalous Proton Conductivity and the Polarizability of Hydrogen Bonds with Tunneling Protons

Cited by 114 publications

References 0 publications

Significant Enhancement of Proton Transport in Bioinspired Peptide Fibrils by Single Acidic or Basic Amino Acid Mutation

Significant Enhancement of Proton Transport in Bioinspired Peptide Fibrils by Single Acidic or Basic Amino Acid Mutation

Analytic treatment of IR-spectroscopy data for double well potential

The F0 complex of the ATP synthase of Escherichia coli contains a proton pathway with large proton polarizability caused by collective proton fluctuation

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