BIOSS-A

Membranes and protein–lipid interactions in signalling
BIOSS-B

Oncogenic signalling
BIOSS-C

Re-building & biotechnology
BIOSS

From Analysis
to Synthesis
Prof. Dr. Oliver Einsle

Prof. Dr. Oliver Einsle
Institute of Biochemistry, University of Freiburg
+49 761 203 6058
10 selected publications
- 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. - 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.