World's Best Scientists 2026 revealed!
Silke Leimkühler

Silke Leimkühler

D-Index & Metrics

Chemistry

D-Index
56
Citations
8749
World Ranking
11901
National Ranking
875

Biology and Biochemistry

D-Index
57
Citations
8787
World Ranking
14089
National Ranking
993

Overview

Silke Leimkühler is affiliated with the University of Potsdam in Germany. The primary focus of their research lies at the intersection of biochemistry, genetics, and molecular biology, with significant contributions also in the field of energy. Their investigations encompass various subfields including renewable energy, sustainability and the environment, molecular biology, materials chemistry, inorganic chemistry, and environmental engineering.

The main topics of their work cover metalloenzymes and iron-sulfur proteins, RNA modifications and cancer, enzyme structure and function, microbial fuel cells and bioremediation, metal-catalyzed oxygenation mechanisms, electrocatalysts for energy conversion, and microbial metabolism and enzyme function.

Leimkühler has published extensively, with notable recent papers including:

  • "Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase," Chemical Reviews, 2022
  • "Cryo-EM structures reveal intricate Fe-S cluster arrangement and charging in Rhodobacter capsulatus formate dehydrogenase," Nature Communications, 2020
  • "Eprenetapopt triggers ferroptosis, inhibits NFS1 cysteine desulfurase, and synergizes with serine and glycine dietary restriction," Science Advances, 2022
  • "Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes," Journal of Biological Chemistry, 2020
  • "The biosynthesis of the molybdenum cofactors in Escherichia coli," Environmental Microbiology, 2020

The frequent co-authors collaborating with Leimkühler include Benjamin R. Duffus, Moses Olalekan Ogunkola, Chantal Iobbi-Nivol, Thomas Happe, and Muhammad Abrar Hasnat. The recurring publication venues for their work are the Journal of Biological Chemistry, Molecules, Journal of Bacteriology, Microbiology Spectrum, and Inorganics.

Leimkühler's research often centers on the structural and functional characterization of enzymes involved in microbial metabolism and energy conversion processes. The work on metalloenzymes and iron-sulfur proteins is a key part of understanding biological catalysis and enzymatic mechanisms essential for energy sustainability and bioremediation applications.

Best Publications

  • Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus

    James J Truglio;Karsten Theis;Silke Leimkühler;Roberto Rappa

  • Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.

    Unknown

  • Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli.

    Chantal Iobbi-Nivol;Silke Leimkühler

  • The oxygen-tolerant and NAD+-dependent formate dehydrogenase from Rhodobacter capsulatus is able to catalyze the reduction of CO2 to formate.

    Tobias Hartmann;Silke Leimkühler

  • Characterization of Escherichia coli MoeB and Its Involvement in the Activation of Molybdopterin Synthase for the Biosynthesis of the Molybdenum Cofactor

    Silke Leimkühler;Margot M. Wuebbens;K.V. Rajagopalan

  • Enzyme cascade reactions: synthesis of furandicarboxylic acid (FDCA) and carboxylic acids using oxidases in tandem

    Shane M. McKenna;Silke Leimkühler;Susanne Herter;Nicholas J. Turner

  • Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans.

    Andreas Matthies;K. V. Rajagopalan;Ralf R. Mendel;Silke Leimkühler

  • A Sulfurtransferase Is Required in the Transfer of Cysteine Sulfur in the in Vitro Synthesis of Molybdopterin from Precursor Z in Escherichia coli

    Silke Leimkühler;K.V. Rajagopalan

  • The History of the Discovery of the Molybdenum Cofactor and Novel Aspects of its Biosynthesis in Bacteria

    Silke Leimkühler;Margot M. Wuebbens;K.V. Rajagopalan

  • Bacterial molybdoenzymes: old enzymes for new purposes

    Silke Leimkühler;Chantal Iobbi-Nivol

  • A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis.

    Zvonimir Marelja;Walter Stöcklein;Manfred Nimtz;Silke Leimkühler

  • The biosynthesis of the molybdenum cofactors

    Ralf R. Mendel;Silke Leimkühler

  • Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulatus is more similar to its eukaryotic counterparts than to prokaryotic molybdenum enzymes.

    Silke Leimkühler;Monika Kern;Peter S. Solomon;Alastair G. McEwan

  • The Sulfurtransferase Activity of Uba4 Presents a Link between Ubiquitin-like Protein Conjugation and Activation of Sulfur Carrier Proteins

    Jennifer Schmitz;Mita Mullick Chowdhury;Petra Hänzelmann;Manfred Nimtz

  • The Impact of Single Nucleotide Polymorphisms on Human Aldehyde Oxidase

    Tobias Hartmann;Mineko Terao;Enrico Garattini;Christian Teutloff

  • The continuous oxidation of HMF to FDCA and the immobilisation and stabilisation of periplasmic aldehyde oxidase (PaoABC)

    S. M. McKenna;P. Mines;P. Law;K. Kovacs-Schreiner

  • Mutations in LYRM4, encoding iron-sulfur cluster biogenesis factor ISD11, cause deficiency of multiple respiratory chain complexes

    Sze Chern Lim;Martin Friemel;Justine E. Marum;Justine E. Marum;Elena J. Tucker;Elena J. Tucker

  • Layer-by-layer arrangement by protein-protein interaction of sulfite oxidase and cytochrome c catalyzing oxidation of sulfite.

    Roman Dronov;Dirk G Kurth;Helmuth Möhwald;Roberto Spricigo

  • Structure and function of mammalian aldehyde oxidases

    Mineko Terao;Maria João Romão;Silke Leimkühler;Marco Bolis

  • Assembly and catalysis of molybdenum or tungsten-containing formate dehydrogenases from bacteria.

    Tobias Hartmann;Nadine Schwanhold;Silke Leimkühler

  • Promoters controlling expression of the alternative nitrogenase and the molybdenum uptake system in Rhodobacter capsulatus are activated by NtrC, independent of sigma54, and repressed by molybdenum.

    M Kutsche;S Leimkühler;S Angermüller;W Klipp

  • Role of XDHC in Molybdenum Cofactor Insertion into Xanthine Dehydrogenase of Rhodobacter capsulatus

    Silke Leimkühler;Werner Klipp

  • Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry.

    Andreas Matthies;Manfred Nimtz;Silke Leimkühler

Frequent Co-Authors

Ulla Wollenberger
Ulla Wollenberger University of Potsdam
Maria João Romão
Maria João Romão Universidade Nova de Lisboa
K. V. Rajagopalan
K. V. Rajagopalan Duke University
Enrico Garattini
Enrico Garattini Mario Negri Institute for Pharmacological Research
Takeshi Nishino
Takeshi Nishino Nippon Medical School
Mineko Terao
Mineko Terao Mario Negri Institute for Pharmacological Research
Michael Haumann
Michael Haumann Freie Universität Berlin
Manfred Nimtz
Manfred Nimtz Helmholtz Centre for Infection Research
Ralf R. Mendel
Ralf R. Mendel Technische Universität Braunschweig
Peter Hildebrandt
Peter Hildebrandt Technical University of Berlin

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