Cluster of Excellence –
University of Freiburg

Prof. Dr. Oliver Einsle

Prof. Dr. Oliver Einsle

Institute of Biochemistry, University of Freiburg

+49 761 203 6058

10 selected publications

  • Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase.
    Spatzal T, Perez KA, Einsle O, Howard JB, Rees DC (2014).
    Science, 345, 1620-1623.
  • Structure and mechanism of the nitrite channel NirC from Salmonella typhimurium.
    Lü W, Schwarzer NJ, Du J, Gerbig-Smentek E, Andrade SLA, Einsle O (2012).
    Proc. Natl. Acad. Sci. USA, 109, 18395-18400.
  • Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor.
    Spatzal T, Aksoyoglu M, Zhang L, Andrade SLA, Schleicher E, Weber S, Rees DC, Einsle O (2011).
    Science, 334, 940.
  • Active site remodeling in the bifunctional fructose-6-bisphosphate aldolase/phosphatase.
    Du J, Say RF, Lü W, Fuchs G, Einsle O (2011).
    Nature, 478, 534-537.
  • N2O binding at a [4Cu:2S] copper-sulfur cluster in nitrous oxide reductase. 
    Pomowski A, Zumft WG, Kroneck PMH, Einsle O (2011).
    Nature 477(7363):234-7
  • pH-dependent gating in a FocA formate channel.
    Lü W, Du J, Wacker T, Gerbig-Smentek E, Andrade SLA, Einsle O (2011).
    Science, 332, 352-354.
  • Crystal Structure of the Archaeal Ammonium Transporter Amt-1 from Archaeoglobus fulgidus.
    Andrade SLA, Dickmanns A, Ficner R, Einsle O (2005). 
    Proc. Natl. Acad. Sci. USA, 102, 14994-14999.
  • Nitrogenase MoFe protein at 1.16 Å resolution: A central ligand in the FeMo cofactor.
    Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC (2002). 
    Science 297, 1696-1700.
  • Implications for metalloprotein assembly from the structure of a FeMo cofactor deficient nitrogenase MoFe protein.
    Schmid B, Ribbe MW, Einsle O, Yoshida M, Thomas LM, Rees DC, Burgess BK (2002). 
    Science 296, 352-356.
  • Structure of cytochrome c nitrite reductase.
    Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PMH (1999). 
    Nature 400, 476-480.