@article{SchiffelsPinkenburgScheldenetal.2013,
  author    = {Schiffels, Johannes and Pinkenburg, Olaf and Schelden, Maximilian and Aboulnaga, El-Hussiny A. A. and Baumann, Marcus and Selmer, Thorsten},
  title     = {An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from cupriavidus necator in Escherichia coli},
  series = {PLOS one. 2013},
  journal   = {PLOS one. 2013},
  publisher = {Public Library of Science},
  address   = {San Francisco, California},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0068812},
  year      = {2013},
  language  = {en}
}
@article{AbulnagaPinkenburgSchiffelsetal.2013,
  author    = {Abulnaga, El-Hussiny and Pinkenburg, Olaf and Schiffels, Johannes and E-Refai, Ahmed and Buckel, Wolfgang and Selmer, Thorsten},
  title     = {Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli},
  series = {Journal of bacteriology},
  volume    = {195},
  journal   = {Journal of bacteriology},
  number    = {16},
  issn      = {1098-5530 [E-Journal]},
  pages     = {3704 -- 3713},
  year      = {2013},
  language  = {en}
}
@article{AboulnagaPinkenburgSchiffelsetal.2013,
  author    = {Aboulnaga, E. H. and Pinkenburg, O. and Schiffels, Johannes and El-Refai, A. and Buckel, W. and Selmer, Thorsten},
  title     = {Butyrate production in Escherichia coli: Exploitation of an oxygen tolerant bifurcating butyryl-CoA dehydrogenase/electron transferring flavoprotein complex from Clostridium difficile},
  series = {Journal of bacteriology. June 14, 2013},
  journal   = {Journal of bacteriology. June 14, 2013},
  issn      = {1098-5530 (E-Journal) ; 0021-9193 (Print)},
  pages     = {Epub ahead of print},
  year      = {2013},
  language  = {de}
}
@inproceedings{KasparGroebelKuperjansetal.2013,
  author    = {Kaspar, K. and Groebel, Simone and Kuperjans, Isabel and Dielmann, Klaus-Peter and Selmer, Thorsten},
  title     = {Charakterisierung der Bioz{\"o}nose von Biogasfermentern in Abh{\"a}ngigkeit verschiedener Substrate},
  series = {Biogas 2013 : 6. Innovationskongress, 23. - 24.05.2013, Osnabr{\"u}ck, Tagungsband},
  booktitle = {Biogas 2013 : 6. Innovationskongress, 23. - 24.05.2013, Osnabr{\"u}ck, Tagungsband},
  publisher = {Profair Consult+Project},
  address   = {Hildesheim},
  issn      = {978-3-9813776-3-7},
  pages     = {69 -- 74},
  year      = {2013},
  language  = {de}
}
@article{HuckSchiffelsHerreraetal.2013,
  author    = {Huck, Christina and Schiffels, Johannes and Herrera, Cony N. and Schelden, Maximilian and Selmer, Thorsten and Poghossian, Arshak and Baumann, Marcus and Wagner, Patrick and Sch{\"o}ning, Michael Josef},
  title     = {Metabolic responses of Escherichia coli upon glucose pulses captured by a capacitive field-effect sensor},
  series = {Physica Status Solidi (A)},
  volume    = {210},
  journal   = {Physica Status Solidi (A)},
  number    = {5},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0031-8965},
  doi       = {10.1002/pssa.201200900},
  pages     = {926 -- 931},
  year      = {2013},
  abstract  = {Living cells are complex biological systems transforming metabolites taken up from the surrounding medium. Monitoring the responses of such cells to certain substrate concentrations is a challenging task and offers possibilities to gain insight into the vitality of a community influenced by the growth environment. Cell-based sensors represent a promising platform for monitoring the metabolic activity and thus, the "welfare" of relevant organisms. In the present study, metabolic responses of the model bacterium Escherichia coli in suspension, layered onto a capacitive field-effect structure, were examined to pulses of glucose in the concentration range between 0.05 and 2 mM. It was found that acidification of the surrounding medium takes place immediately after glucose addition and follows Michaelis-Menten kinetic behavior as a function of the glucose concentration. In future, the presented setup can, therefore, be used to study substrate specificities on the enzymatic level and may as well be used to perform investigations of more complex metabolic responses. Conclusions and perspectives highlighting this system are discussed.},
  language  = {en}
}