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Chemistry

D-Index
57
Citations
15234
World Ranking
10946
National Ranking
788

Research.com Recognitions

  • 2020 - German National Academy of Sciences Leopoldina - Deutsche Akademie der Naturforscher Leopoldina – Nationale Akademie der Wissenschaften Biochemistry and Biophysics

Overview

Oliver Einsle is affiliated with the University of Freiburg in Germany, specializing in biochemical and molecular biology research with a focus on energy-related processes. Their work spans multiple subfields, including molecular biology, renewable energy and sustainability, materials chemistry, inorganic chemistry, and catalysis.

The main fields of study for Einsle include biochemistry, genetics, and molecular biology, alongside significant contributions to the energy sector. Specific research topics encompass:

  • Metalloenzymes and iron-sulfur proteins
  • Photosynthetic processes and mechanisms
  • Ammonia synthesis and nitrogen reduction
  • Microbial fuel cells and bioremediation
  • Enzyme structure and function
  • Electrocatalysts for energy conversion
  • Metal-catalyzed oxygenation mechanisms

Einsle's publication record features work in several prominent scientific venues. Their frequent publication outlets include:

  • Journal of Medicinal Chemistry
  • ChemBioChem
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Angewandte Chemie International Edition
  • Nature Communications

Recent notable papers authored or coauthored by Einsle cover enzymology and catalysis topics:

  • Structural Enzymology of Nitrogenase Enzymes (2020, Chemical Reviews)
  • 2022 Roadmap on Low Temperature Electrochemical CO2 Reduction (2022, Journal of Physics Energy)
  • Iron-only Fe-nitrogenase Underscores Common Catalytic Principles in Biological Nitrogen Fixation (2023, Nature Catalysis)
  • CO Binding to the FeV Cofactor of CO-Reducing Vanadium Nitrogenase at Atomic Resolution (2020, Angewandte Chemie International Edition)
  • Two Ligand-Binding Sites in CO-Reducing V Nitrogenase Reveal a General Mechanistic Principle (2021, Science Advances)

Einsle collaborates frequently with several researchers in their field. Regular coauthors include:

  • Lin Zhang
  • Manfred Jung
  • Stefan Günther
  • Wolfgang Sippl
  • S. Gerhardt

In 2020, Oliver Einsle was recognized by the German National Academy of Sciences Leopoldina for contributions in biochemistry and biophysics.

Best Publications

  • Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.

    Oliver Einsle;Oliver Einsle;F. Akif Tezcan;Susana L. A. Andrade;Susana L. A. Andrade;Benedikt Schmid

  • Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor

    Thomas Spatzal;Müge Aksoyoglu;Limei Zhang;Susana L. A. Andrade

  • Anaerobic Microbial Degradation of Hydrocarbons : from Enzymatic Reactions to the Environment

    Ralf Rabus;Matthias Boll;Johann Heider;Rainer U. Meckenstock

  • Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase

    Thomas Spatzal;Kathryn A. Perez;Oliver Einsle;James B. Howard;James B. Howard

  • Structure of cytochrome c nitrite reductase

    Oliver Einsle;Albrecht Messerschmidt;Petra Stach;Gleb P. Bourenkov

  • Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase.

    Oliver Einsle;Albrecht Messerschmidt;Robert Huber;Peter M. H. Kroneck

  • Structural basis of biological nitrogen fixation

    Douglas C Rees;F Akif Tezcan;Chad A Haynes;Mika Y Walton

  • Structural Enzymology of Nitrogenase Enzymes

    Oliver Einsle;Douglas C. Rees

  • The structure of vanadium nitrogenase reveals an unusual bridging ligand

    Daniel Sippel;Oliver Einsle

  • Selective Sirt2 inhibition by ligand-induced rearrangement of the active site.

    Tobias Rumpf;Matthias Schiedel;Berin Karaman;Claudia Roessler

  • A bound reaction intermediate sheds light on the mechanism of nitrogenase

    Daniel Sippel;Michael Rohde;Julia Netzer;Christian Trncik

  • Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus

    Susana L. A. Andrade;Antje Dickmanns;Ralf Ficner;Oliver Einsle

  • Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs.

    Oliver Einsle;Oliver Einsle;Petra Stach;Albrecht Messerschmidt;Jörg Simon

  • N2O binding at a [4Cu:2S] copper-sulphur cluster in nitrous oxide reductase.

    Anja Pomowski;Walter G. Zumft;Peter M. H. Kroneck;Oliver Einsle

  • Structure of a Cofactor-Deficient Nitrogenase MoFe Protein

    Benedikt Schmid;Markus W. Ribbe;Oliver Einsle;Mika Yoshida

  • A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes.

    Jörg Simon;Roland Gross;Oliver Einsle;Oliver Einsle;Peter M. H. Kroneck

  • Identification of a spin-coupled Mo(III) in the nitrogenase iron–molybdenum cofactor

    Ragnar Bjornsson;Frederico A. Lima;Thomas Spatzal;Thomas Weyhermüller

  • Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement

    Thomas Spatzal;Thomas Spatzal;Julia Schlesier;Eva Maria Burger;Daniel Sippel

  • Direct Reductive Amination of Ketones: Structure and Activity of S-Selective Imine Reductases from Streptomyces.

    Tobias Huber;Lisa Schneider;Andreas Präg;Stefan Gerhardt

  • The Amt/Mep/Rh family of ammonium transport proteins.

    Susana L A Andrade;Oliver Einsle

Frequent Co-Authors

Peter M. H. Kroneck
Peter M. H. Kroneck University of Konstanz
Douglas C. Rees
Douglas C. Rees California Institute of Technology
Albrecht Messerschmidt
Albrecht Messerschmidt Max Planck Society
Manfred Jung
Manfred Jung University of Freiburg
Serena DeBeer
Serena DeBeer Max Planck Society
Thorsten Friedrich
Thorsten Friedrich University of Freiburg
Marcellus Ubbink
Marcellus Ubbink Leiden University
Wolfgang Sippl
Wolfgang Sippl Martin Luther University Halle-Wittenberg
James B. Howard
James B. Howard University of Minnesota
Gerard W. Canters
Gerard W. Canters Leiden University

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