Publications by authors named "Stephan Rein"

Flavocoenzymes are nearly ubiquitous cofactors that are involved in the catalysis and regulation of a wide range of biological processes including some light-induced ones, such as the photolyase-mediated DNA repair, magnetoreception of migratory birds, and the blue-light driven phototropism in plants. One of the factors that enable versatile flavin-coenzyme biochemistry and biophysics is the fine-tuning of the cofactor's frontier orbital by interactions with the protein environment. Probing the singly-occupied molecular orbital (SOMO) of the intermediate radical state of flavins is therefore a prerequisite for a thorough understanding of the diverse functions of the flavoprotein family.

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The Cytotoxic Necrotizing Factor Y (CNFY) is produced by the gram-negative, enteric pathogen Yersinia pseudotuberculosis. The bacterial toxin belongs to a family of deamidases, which constitutively activate Rho GTPases, thereby balancing inflammatory processes. We identified heparan sulfate proteoglycans as essential host cell factors for intoxication with CNFY.

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The perfluorinated dihydrophenazine derivative (perfluoro-5,10-bis(perfluorophenyl)-5,10-dihydrophenazine) ("phenazine ") can be easily transformed to a stable and weighable radical cation salt by deelectronation (i.e. oxidation) with Ag[Al(OR ) ]/ Br mixtures (R =C(CF ) ).

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Fluorescence resonance energy transfer in single enzyme molecules (smFRET, single-molecule measurement) allows the measurement of multicomponent distance distributions in complex biomolecules similar to pulsed electron-electron double resonance (PELDOR, ensemble measurement). Both methods use reporter groups: FRET exploits the distance dependence of the electric interaction between electronic transition dipole moments of the attached fluorophores, whereas PELDOR spectroscopy uses the distance dependence of the interaction between the magnetic dipole moments of attached spin labels. Such labels can be incorporated easily to cysteine residues in the protein.

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Pulsed electron-electron double resonance (PELDOR, alternatively called DEER for double electron-electron resonance) pulse sequences allow for the detection of echo decay curves that are modulated by dipole-dipole-coupling frequencies of interacting electron spins. With increasing distance between them, the echo decay needs to be monitored over a progressively extended time period. However, since the echo intensity typically falls off exponentially with increasing time, this might be problematic with respect to the minimum signal-to-noise ratio required for a sound data analysis.

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While it is often longed for very gentle oxidising agents with ideally close to no interaction with the generated substrate, it may sometimes be beneficial to have an oxidising agent at hand which is able to stabilise a reactive species directly after its generation. Here we present the synthesis of the hexamethylbenzene radical cation as a ligand forming oxidising agent. Its utility was demonstrated by the exemplarily chosen access to the mono-arene complex-cations of univalent gallium and indium [M(C6Me6)]+[Al(ORF)4]- (M = Ga and In).

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Time-resolved electron paramagnetic resonance (TREPR) spectroscopy is shown to be a powerful tool to characterize triplet excitons of conjugated polymers. The resulting spectra are highly sensitive to the orientation of the molecule. In thin films cast on PET film, the molecules' orientation with respect to the surface plane can be determined, providing access to sample morphology on a microscopic scale.

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The dinuclear doubly azole-bridged copper(II) complexes [Cu(II)2(L)2(MeCN)4](ClO4)4·3.73MeCN·0.80H2O and [Cu(II)2(L)6](ClO4)4·solvent (solvent = 2MeCN·H2O; 2MeCN·2H2O; 1.

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