In: ChemBioChem, 2018, vol. 19, no. 9, p. 922–926
In nature, proteins serve as media for long‐distance electron transfer (ET) to carry out redox reactions in distant compartments. This ET occurs either by a single‐step superexchange or through a multi‐step charge hopping process, which uses side chains of amino acids as stepping stones. In this study we demonstrate that Phe can act as a relay amino acid for long‐distance electron...
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In: Journal of Physical Organic Chemistry, 2015, vol. 28, no. 5, p. 347–353
Long distance electron transfer in proteins requires relay stations that can be transitorily oxidized or reduced. Although individual prolines cannot assume this function, because of their high ionization energy, it has been shown that polyprolines have the ability to transfer charges. In order to determine the role of the proline in the hole distribution and transport within a PheProPhe...
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In: Angewandte Chemie International Edition, 2015, vol. 54, no. 10, p. 2912–2916
Some microorganisms perform anaerobic mineral respiration by reducing metal ions to metal nanoparticles, using peptide aggregates as medium for electron transfer (ET). Such a reaction type is investigated here with model peptides and silver as the metal. Surprisingly, Ag⁺ ions bound by peptides with histidine as the Ag⁺-binding amino acid and tyrosine as photoinducible electron donor cannot...
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In: The Journal of Physical Chemistry B, 2014, vol. 118, no. 16, p. 4261–4272
Charge transfer in peptides and proteins can occur on different pathways, depending on the energetic landscape as well as the coupling between the involved orbitals. Since details of the mechanism and pathways are difficult to access experimentally, different modeling strategies have been successfully applied to study these processes in the past. These can be based on a simple empirical pathway...
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In: Chemical Reviews, 2013, vol. 113, no. 7, p. 4708–4754
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In: Angewandte Chemie International Edition, 2013, vol. 52, no. 17, p. 4682–4685
Single-crystal to single-crystal transformations are possible by ion-exchange and transport reactions through supramolecular channels that are composed of crown ether molecules and use trihalide ions as scaffolds. Kinetic measurements of ion transport at different temperatures provide activation energy data and show that a very fast.
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In: Chimia, 2012, vol. 66, no. 6, p. 364-367
Electron transfer (ET) through peptides and proteins is a key biochemical process, which involves radicals and radical ions as reactive intermediates. We have developed an assay that allows us to study this fundamental chemical reaction.
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In: Physical Chemistry Chemical Physics, 2012, vol. 14, no. 40, p. 13785-13788
The life time of aromatic radical cations is limited by reactions like β-elimination, dimerization, and addition to the solvent. Here we show that the attachment of such a radical cation to the C-terminal end of an α-/3₁₀-helical peptide further reduces its life time by two orders of magnitude. For PPII-helical peptides, such an effect is only observed if the peptide contains an adjacent...
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In: The Journal of Physical Chemistry B, 2012, vol. 116, p. 2284–2293
Charge transfer within and between biomolecules remains a highly active field of biophysics. Due to the complexities of real systems, model compounds are a useful alternative to study the mechanistic fundamentals of charge transfer. In recent years, such model experiments have been underpinned by molecular simulation methods as well. In this work, we study electron hole transfer in helical model...
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In: Angewandte Chemie International Edition, 2011, vol. 50, no. 8, p. 1926-1930
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