@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}
}
@article{TrautweinFredrikssonMoelleretal.2016,
  author    = {Trautwein, Matthias and Fredriksson, Kai and M{\"o}ller, Heiko Michael and Exner, Thomas E.},
  title     = {Automated assignment of NMR chemical shifts based on a known structure and 4D spectra},
  series = {Journal of biomolecular NMR},
  volume    = {65},
  journal   = {Journal of biomolecular NMR},
  publisher = {Springer},
  address   = {Dordrecht},
  issn      = {0925-2738},
  doi       = {10.1007/s10858-016-0050-0},
  pages     = {217 -- 236},
  year      = {2016},
  abstract  = {Apart from their central role during 3D structure determination of proteins the backbone chemical shift assignment is the basis for a number of applications, like chemical shift perturbation mapping and studies on the dynamics of proteins. This assignment is not a trivial task even if a 3D protein structure is known and needs almost as much effort as the assignment for structure prediction if performed manually. We present here a new algorithm based solely on 4D [H-1, N-15]-HSQC-NOESY-[H-1, N-15]-HSQC spectra which is able to assign a large percentage of chemical shifts (73-82 \%) unambiguously, demonstrated with proteins up to a size of 250 residues. For the remaining residues, a small number of possible assignments is filtered out. This is done by comparing distances in the 3D structure to restraints obtained from the peak volumes in the 4D spectrum. Using dead-end elimination, assignments are removed in which at least one of the restraints is violated. Including additional information from chemical shift predictions, a complete unambiguous assignment was obtained for Ubiquitin and 95 \% of the residues were correctly assigned in the 251 residue-long N-terminal domain of enzyme I. The program including source code is available at https://github.com/thomasexner/4Dassign.},
  language  = {en}
}
@article{PrestelMoeller2016,
  author    = {Prestel, Andreas and M{\"o}ller, Heiko Michael},
  title     = {Spatio-temporal control of cellular uptake achieved by photoswitchable cell-penetrating peptides},
  series = {Chemical communications},
  volume    = {52},
  journal   = {Chemical communications},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1359-7345},
  doi       = {10.1039/c5cc06848g},
  pages     = {701 -- 704},
  year      = {2016},
  abstract  = {The selective uptake of compounds into specific cells of interest is a major objective in cell biology and drug delivery. By incorporation of a novel, thermostable azobenzene moiety we generated peptides that can be switched optically between an inactive state and an active, cell-penetrating state with excellent spatio-temporal control.},
  language  = {en}
}
@article{MaierPoluektovJesteretal.2016,
  author    = {Maier, Stefan K. and Poluektov, Georgiy and Jester, Stefan-S. and M{\"o}ller, Heiko Michael and Hoeger, Sigurd},
  title     = {Fast Oxidative Cyclooligomerization towards Low- and High-Symmetry Thiophene Macrocycles},
  series = {Chemistry - a European journal},
  volume    = {22},
  journal   = {Chemistry - a European journal},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0947-6539},
  doi       = {10.1002/chem.201503211},
  pages     = {1379 -- 1384},
  year      = {2016},
  abstract  = {Macrocycles with quaterthiophene subunits were obtained by cyclooligomerization by direct oxidative coupling of unsubstituted dithiophene moieties. The rings were closed with high selectivity by an \&\#945;,\&\#946;\&\#8242;-connection of the thiophenes as proven by NMR spectroscopy. The reaction of the precursor with terthiophene moieties yielded the symmetric \&\#945;,\&\#945;\&\#8242;-linked macrocycle in low yield together with various differently connected isomers. Blocking of the \&\#946;-position of the half-rings yielded selectively the \&\#945;,\&\#945;\&\#8242;-linked macrocycle. Selected cyclothiophenes were investigated by scanning tunneling microscopy, which displayed the formation of highly ordered 2D crystalline monolayers.},
  language  = {en}
}
@article{HolertYuecelJagmannetal.2016,
  author    = {Holert, Johannes and Y{\"u}cel, Onur and Jagmann, Nina and Prestel, Andreas and M{\"o}ller, Heiko Michael and Philipp, Bodo},
  title     = {Identification of bypass reactions leading to the formation of one central steroid degradation intermediate in metabolism of different bile salts in Pseudomonas sp strain Chol1},
  series = {Environmental microbiology},
  volume    = {18},
  journal   = {Environmental microbiology},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1462-2912},
  doi       = {10.1111/1462-2920.13192},
  pages     = {3373 -- 3389},
  year      = {2016},
  language  = {en}
}