@article{ToulouseSchmuckerMeteschetal.2019,
  author    = {Toulouse, Charlotte Marguerite and Schmucker, Sonja and Metesch, Kristina and Pfannstiel, Jens and Michel, Bernd and Starke, Ines and M{\"o}ller, Heiko Michael and Stefanski, Volker and Steuber, Julia},
  title     = {Mechanism and impact of catecholamine conversion by Vibrio cholerae},
  series = {Biochimica et biophysica acta : Bioenergetics},
  volume    = {1860},
  journal   = {Biochimica et biophysica acta : Bioenergetics},
  number    = {6},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {0005-2728},
  doi       = {10.1016/j.bbabio.2019.04.003},
  pages     = {478 -- 487},
  year      = {2019},
  abstract  = {Bacterial pathogens are influenced by signaling molecules including the catecholamines adrenaline and noradrenaline which are host-derived hormones and neurotransmitters. Adrenaline and noradrenaline modulate growth, motility and virulence of bacteria. We show that adrenaline is converted by the pathogen Vibrio cholerae to adrenochrome in the course of respiration, and demonstrate that superoxide produced by the respiratory, Na+ - translocating NADH:quinone oxidoreductase (NQR) acts as electron acceptor in the oxidative conversion of adrenaline to adrenochrome. Adrenochrome stimulates growth of V. cholerae, and triggers specific responses in V. cholerae and in immune cells. We performed a quantitative proteome analysis of V. cholerae grown in minimal medium with glucose as carbon source without catecholamines, or with adrenaline, noradrenaline or adrenochrome. Significant regulation of proteins participating in iron transport and iron homeostasis, in energy metabolism, and in signaling was observed upon exposure to adrenaline, noradrenaline or adrenochrome. On the host side, adrenochrome inhibited lipopolysaccharide-triggered formation of TNF-alpha by THP-1 monocytes, though to a lesser extent than adrenaline. It is proposed that adrenochrome produced from adrenaline by respiring V. cholerae functions as effector molecule in pathogen-host interaction.},
  language  = {en}
}
@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}
}
@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}
}
@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}
}