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Prof. Dr. Oliver Einsle
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Academic Career Length
28Years (1999-Present)
(Calculated once Scilit publication data is synced: current year − year of first publication + 1)
Representative Publications
View All Publications6 September 2002 in Science
Journal Article
OEOliver Einsle
Oliver EinsleFTF. Akif Tezcan
F. Akif Tezcan
SASusana L. A. Andrade
Susana L. A. Andrade
BSBenedikt Schmid
Benedikt Schmid
MYMika Yoshida
Mika Yoshida
DRDouglas C. Rees
Douglas C. Rees
+1
A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase.
18 November 2011 in Science
Journal Article
TSThomas Spatzal
Thomas Spatzal
MAMüge Aksoyoglu
Müge Aksoyoglu
LZLimei Zhang
Limei Zhang
SASusana L. A. Andrade
Susana L. A. Andrade
ESErik Schleicher
Erik Schleicher
OEOliver Einsle
Oliver Einsle +2
Structural data show that the light atom at the center of the nitrogenase active site cofactor is a carbon.
15 June 2020 in Chemical Reviews
Journal Article
OEOliver Einsle
Oliver EinsleDRDouglas C. Rees
Douglas C. Rees26 September 2014 in Science
Journal Article
TSThomas Spatzal
Thomas SpatzalKPKathryn A. Perez
Kathryn A. Perez
OEOliver Einsle
Oliver EinsleJHJames B. Howard
James B. Howard
DRDouglas C. Rees
Douglas C. ReesMaking nitrogen available for biosynthesis: Nitrogen gas (N 2 ) is abundant in Earth's atmosphere; however, it must be converted into a bioavailable form before it can be incorporated into biomolecules. The enzyme nitrogenase, which is made up of two metalloproteins, converts N 2 into bioavailable ammonia. One of these, the MoFe-protein, contains a complex metal center, the FeMo cofactor, where the triple N 2 bond is reduced. Understanding how nitrogenase achieves the reduction of N 2 has been a long-term goal. Spatzal et al. present the structure of MoFe-protein bound to carbon monoxide (see the Perspective by Hogbom). Although this is an inhibitor rather than the natural substrate, the structure gives insight into how the FeMo metallocluster rearranges to achieve substrate reduction. Science , this issue p. 1620
1 July 1999 in Nature
Journal Article
OEOliver Einsle
Oliver EinsleAMAlbrecht Messerschmidt
Albrecht Messerschmidt
PSPetra Stach
Petra Stach
GBGleb P. Bourenkov
Gleb P. BourenkovHBHans D. Bartunik
Hans D. Bartunik
PKPeter M. H. Kroneck
Peter M. H. Kroneck
+1
7 September 2002 in Journal of the American Chemical Society
Journal Article
OEOliver Einsle
Oliver EinsleAMAlbrecht Messerschmidt
Albrecht Messerschmidt
RHRobert Huber
Robert Huber
PKPeter M. H. Kroneck
Peter M. H. Kroneck
FNFrank Neese
Frank NeeseAbout Me
Prof. Dr. Oliver Einsle studied Biology in Konstanz, Germany, and then moved to the Max-Planck Institute for Biochemistry in Martinsried, Germany, to work with Robert Huber and Peter Kroneck on cytochrome c nitrite reductase. In 2001, he joined the laboratory of Douglas Rees at Caltech, USA, to study nitrogenase, and in 2003, he was appointed junior professor for protein crystallography in Göttingen, Germany. Since 2008, he has been a full professor of Biochemistry in Freiburg, Germany, and director of the Institute of Biochemistry in the faculty of Chemistry and Pharmacy. His group has made seminal contributions to the structural and functional characterization of various metalloproteins, including nitrogenase and nitrous
oxide reductase, but also multiheme cytochromes c. A second line of research is centered on the study of integral membrane proteins, in particular, bacterial transporters and channels.