@article{StarkeKochKammeretal.2018,
  author    = {Starke, Ines and Koch, Andreas and Kammer, Stefan and Holdt, Hans-J{\"u}rgen and M{\"o}ller, Heiko Michael},
  title     = {Electrospray mass spectrometry and molecular modeling study of formation and stability of silver complexes with diazaperylene and bisisoquinoline},
  series = {Journal of mass spectrometry},
  volume    = {53},
  journal   = {Journal of mass spectrometry},
  number    = {5},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {1076-5174},
  doi       = {10.1002/jms.4071},
  pages     = {408 -- 418},
  year      = {2018},
  abstract  = {The complex formation of the following diazaperylene ligands (L) 1,12-diazaperylene 1, 1,1-bisisoquinoline 2, 2,11-disubstituted 1,12-diazaperylenes (alkyl=methyl, ethyl, isopropyl, 3, 5, 7), 3,3-disubstituted 1,1-bisisoquinoline (alkyl=methyl, ethyl, isopropyl, 4, 6, 8 and with R=phenyl, 11 and with pyridine 12), and the 5,8-dimethoxy-substituted diazaperylene 9, 6,6-dimethoxy-substituted bisisoquinoline 10 with AgBF4 was investigated. Collision-induced dissociation measurements were used to evaluate the relative stabilities of the ligands themselves and for the [1:1](+) complexes as well as for the homoleptic and heteroleptic silver [1:2](+) complexes in the gas phase. This method is very useful in rapid screening of the stabilities of new complexes in the gas phase. The influence of the spatial arrangement of the ligands and the type of substituents employed for the complexation were examined. The effect of the preorganization of the diazaperylene on the threshold activation voltages and thus of the relative binding energies of the different complexes are discussed. Density functional theory calculations were used to calculate the optimized structures of the silver complexes and compared with the stabilities of the complexes in the gas phase for the first time.},
  language  = {en}
}
@article{MadaniAnghileriHeydenreichetal.2022,
  author    = {Madani, Amiera and Anghileri, Lucia and Heydenreich, Matthias and M{\"o}ller, Heiko Michael and Pieber, Bartholom{\"a}us},
  title     = {Benzylic fluorination induced by a charge-transfer complex with a solvent-dependent selectivity switch},
  series = {Organic letters / publ. by the American Chemical Society},
  volume    = {24},
  journal   = {Organic letters / publ. by the American Chemical Society},
  number    = {29},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1523-7060},
  doi       = {10.1021/acs.orglett.2c02050},
  pages     = {5376 -- 5380},
  year      = {2022},
  abstract  = {We present a divergent strategy for the fluorination of phenylacetic acid derivatives that is induced by a charge-transfer complex between Selectfluor and 4-(dimethylamino)pyridine. A comprehensive investigation of the conditions revealed a critical role of the solvent on the reaction outcome. In the presence of water, decarboxylative fluorination through a single-electron oxidation is dominant. Non-aqueous conditions result in the clean formation of alpha-fluoro-alpha-arylcarboxylic acids.},
  language  = {en}
}
@article{SamahaHamdoCongetal.2020,
  author    = {Samaha, Doaa and Hamdo, Housam H. and Cong, Xiaojing and Schumacher, Fabian and Banhart, Sebastian and Aglar, {\"O}znur and M{\"o}ller, Heiko Michael and Heuer, Dagmar and Kleuser, Burkhard and Saied, Essa M. and Arenz, Christoph},
  title     = {Liposomal FRET assay identifies potent drug-like inhibitors of the Ceramide Transport Protein (CERT)},
  series = {Chemistry - a European journal},
  volume    = {26},
  journal   = {Chemistry - a European journal},
  number    = {70},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0947-6539},
  doi       = {10.1002/chem.202003283},
  pages     = {16616 -- 16621},
  year      = {2020},
  abstract  = {Ceramide transfer protein (CERT) mediates non-vesicular transfer of ceramide from endoplasmic reticulum to Golgi apparatus and thus catalyzes the rate-limiting step of sphingomyelin biosynthesis. Usually, CERT ligands are evaluated in tedious binding assays or non-homogenous transfer assays using radiolabeled ceramides. Herein, a facile and sensitive assay for CERT, based on Forster resonance energy transfer (FRET), is presented. To this end, we mixed donor and acceptor vesicles, each containing a different fluorescent ceramide species. By CERT-mediated transfer of fluorescent ceramide, a FRET system was established, which allows readout in 96-well plate format, despite the high hydrophobicity of the components. Screening of a 2 000 compound library resulted in two new potent CERT inhibitors. One is approved for use in humans and one is approved for use in animals. Evaluation of cellular activity by quantitative mass spectrometry and confocal microscopy showed inhibition of ceramide trafficking and sphingomyelin biosynthesis.},
  language  = {en}
}
@article{VorburgerNedielkovBrosigetal.2016,
  author    = {Vorburger, Thomas and Nedielkov, Ruslan and Brosig, Alexander and Bok, Eva and Schunke, Emina and Steffen, Wojtek and Mayer, Sonja and Goetz, Friedrich and M{\"o}ller, Heiko Michael and Steuber, Julia},
  title     = {Role of the Na+-translocating NADH:quinone oxidoreductase in voltage generation and Na+ extrusion in Vibrio cholerae},
  series = {Biochimica et biophysica acta : Bioenergetics},
  volume    = {1857},
  journal   = {Biochimica et biophysica acta : Bioenergetics},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0005-2728},
  doi       = {10.1016/j.bbabio.2015.12.010},
  pages     = {473 -- 482},
  year      = {2016},
  abstract  = {For Vibrio cholerae, the coordinated import and export of Na+ is crucial for adaptation to habitats with different osmolarities. We investigated the Na+-extruding branch of the sodium cycle in this human pathogen by in vivo Na-23-NMR spectroscopy. The Na+ extrusion activity of cells was monitored after adding glucose which stimulated respiration via the Na+-translocating NADH:quinone oxidoreductase (Na+-NQR). In a V. cholerae deletion mutant devoid of the Na+-NQR encoding genes (nqrA-F), rates of respiratory Na+ extrusion were decreased by a factor of four, but the cytoplasmic Na+ concentration was essentially unchanged. Furthermore, the mutant was impaired in formation of transmembrane voltage (Delta psi, inside negative) and did not grow under hypoosmotic conditions at pH 8.2 or above. This growth defect could be complemented by transformation with the plasmid encoded nqr operon. In an alkaline environment, Na+/H+ antiporters acidify the cytoplasm at the expense of the transmembrane voltage. It is proposed that, at alkaline pH and limiting Na+ concentrations, the Na+-NQR is crucial for generation of a transmembrane voltage to drive the import of H+ by electrogenic Na+/H+ antiporters. Our study provides the basis to understand the role of the Na+-NQR in pathogenicity of V. cholerae and other pathogens relying on this primary Na+ pump for respiration. (C) 2015 Elsevier B.V. All rights reserved.},
  language  = {en}
}
@inproceedings{RamadanGuerreroNedielkovetal.2021,
  author    = {Ramadan, Shahenda and Guerrero, Paula and Nedielkov, Ruslan and Klishin, Nikolai and Dimova, Rumiana and Silva, Daniel V. and M{\"o}ller, Heiko},
  title     = {Building a mimetic system for unraveling protein-protein interactions on membranes},
  series = {European biophysics journal : with biophysics letters ; an international journal of biophysics},
  volume    = {50},
  booktitle = {European biophysics journal : with biophysics letters ; an international journal of biophysics},
  number    = {SUPPL 1},
  publisher = {Springer},
  address   = {Berlin ; Heidelberg ; New York},
  issn      = {0175-7571},
  doi       = {10.1007/s00249-021-01558-w},
  pages     = {S153 -- S153},
  year      = {2021},
  language  = {en}
}