Prof. Dr. Oliver Einsle

10 selected publications

• Molecular interplay of an assembly machinery for nitrous oxide reductase.
  Müller C, Zhang L, Zipfel S, Topitsch A, Lutz M, Eckert J, Prasser B, Chami M, Lü W, Du J, Einsle O (2022).
  Nature, 606, 626-632.
• A bound reaction intermediate sheds light on the mechanism of nitrogenase.
  Sippel D, Rohde M, Netzer J, Trncik C, Gies J, Grunau K, Djurdjevic I, Decamps L, Andrade SLA, Einsle O (2018).
  Science, 359, 1484-1489.
• The octahaem MccA is a haem c–copper sulphite reductase.
  Hermann B, Kern M, La Pietra L, Simon J, Einsle O (2015).
  Nature, 520, 706-709.
• 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.
• 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.
• 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.
• 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.