@article{MuellerNedielkovArndt2022,
  author    = {M{\"u}ller, Marik and Nedielkov, Ruslan and Arndt, Katja M.},
  title     = {Strategies for Enzymatic Inactivation of the Veterinary Antibiotic Florfenicol},
  series = {Antibiotics},
  volume    = {11},
  journal   = {Antibiotics},
  number    = {4},
  publisher = {MDPI},
  address   = {Basel, Schweiz},
  issn      = {2079-6382},
  doi       = {10.3390/antibiotics11040443},
  pages     = {1 -- 18},
  year      = {2022},
  abstract  = {Large quantities of the antibiotic florfenicol are used in animal farming and aquaculture, contaminating the ecosystem with antibiotic residues and promoting antimicrobial resistance, ultimately leading to untreatable multidrug-resistant pathogens. Florfenicol-resistant bacteria often activate export mechanisms that result in resistance to various structurally unrelated antibiotics. We devised novel strategies for the enzymatic inactivation of florfenicol in different media, such as saltwater or milk. Using a combinatorial approach and selection, we optimized a hydrolase (EstDL136) for florfenicol cleavage. Reaction kinetics were followed by time-resolved NMR spectroscopy. Importantly, the hydrolase remained active in different media, such as saltwater or cow milk. Various environmentally-friendly application strategies for florfenicol inactivation were developed using the optimized hydrolase. As a potential filter device for cost-effective treatment of waste milk or aquacultural wastewater, the hydrolase was immobilized on Ni-NTA agarose or silica as carrier materials. In two further application examples, the hydrolase was used as cell extract or encapsulated with a semi-permeable membrane. This facilitated, for example, florfenicol inactivation in whole milk, which can help to treat waste milk from medicated cows, to be fed to calves without the risk of inducing antibiotic resistance. Enzymatic inactivation of antibiotics, in general, enables therapeutic intervention without promoting antibiotic resistance.},
  language  = {en}
}
@misc{MuellerNedielkovArndt2022,
  author    = {M{\"u}ller, Marik and Nedielkov, Ruslan and Arndt, Katja M.},
  title     = {Strategies for Enzymatic Inactivation of the Veterinary Antibiotic Florfenicol},
  series = {Zweitver{\"o}ffentlichungen der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Zweitver{\"o}ffentlichungen der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  publisher = {Universit{\"a}tsverlag Potsdam},
  address   = {Potsdam},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-56162},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-561621},
  pages     = {1 -- 18},
  year      = {2022},
  abstract  = {Large quantities of the antibiotic florfenicol are used in animal farming and aquaculture, contaminating the ecosystem with antibiotic residues and promoting antimicrobial resistance, ultimately leading to untreatable multidrug-resistant pathogens. Florfenicol-resistant bacteria often activate export mechanisms that result in resistance to various structurally unrelated antibiotics. We devised novel strategies for the enzymatic inactivation of florfenicol in different media, such as saltwater or milk. Using a combinatorial approach and selection, we optimized a hydrolase (EstDL136) for florfenicol cleavage. Reaction kinetics were followed by time-resolved NMR spectroscopy. Importantly, the hydrolase remained active in different media, such as saltwater or cow milk. Various environmentally-friendly application strategies for florfenicol inactivation were developed using the optimized hydrolase. As a potential filter device for cost-effective treatment of waste milk or aquacultural wastewater, the hydrolase was immobilized on Ni-NTA agarose or silica as carrier materials. In two further application examples, the hydrolase was used as cell extract or encapsulated with a semi-permeable membrane. This facilitated, for example, florfenicol inactivation in whole milk, which can help to treat waste milk from medicated cows, to be fed to calves without the risk of inducing antibiotic resistance. Enzymatic inactivation of antibiotics, in general, enables therapeutic intervention without promoting antibiotic resistance.},
  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}
}