Her primary areas of study are Biochemistry, Molybdenum cofactor, Molybdopterin, Rhodobacter and Cofactor. She focuses mostly in the field of Biochemistry, narrowing it down to matters related to Stereochemistry and, in some cases, Oxidoreductase and Active site. Her Molybdenum cofactor study integrates concerns from other disciplines, such as Amino acid, Molecular biology and Protein subunit.
Within one scientific family, Silke Leimkühler focuses on topics pertaining to Peptide sequence under Molybdopterin, and may sometimes address concerns connected to Cofactor binding, Molybdopterin synthase and Molecular mass. Her studies examine the connections between Rhodobacter and genetics, as well as such issues in NAD+ kinase, with regards to Formate dehydrogenase, Formate and Formate oxidation. Her work carried out in the field of Cofactor brings together such families of science as Nitrogen assimilation, Bacteria, Anaerobic respiration and Metalloprotein.
Silke Leimkühler mainly investigates Biochemistry, Molybdenum cofactor, Cofactor, Molybdopterin and Enzyme. Her research related to Biosynthesis, Rhodobacter, Escherichia coli, Xanthine dehydrogenase and Aldehyde oxidase might be considered part of Biochemistry. The various areas that Silke Leimkühler examines in her Molybdenum cofactor study include Molybdenum, Sulfurtransferase, Protein subunit, Stereochemistry and Transfer RNA.
Her study looks at the relationship between Stereochemistry and topics such as Active site, which overlap with Substrate. Her research investigates the connection between Cofactor and topics such as Oxidoreductase that intersect with issues in Aldehyde and Redox. Silke Leimkühler has included themes like Cysteine, Nucleotide and Sulfite oxidase in her Molybdopterin study.
Her scientific interests lie mostly in Biochemistry, Molybdenum cofactor, Enzyme, Stereochemistry and Escherichia coli. Her study in Molybdenum cofactor is interdisciplinary in nature, drawing from both Transfer RNA, Xanthine dehydrogenase, Molybdopterin and Bacteria. Her Enzyme study combines topics from a wide range of disciplines, such as Amino acid and Metabolism.
Her Stereochemistry research is multidisciplinary, relying on both Molybdenum, Formate dehydrogenase, Cofactor, Pterin and Ligand. Her work deals with themes such as Rhodobacter, Cysteine and Guanine, which intersect with Cofactor. The Escherichia coli study combines topics in areas such as Plasma protein binding, Iron–sulfur cluster, Chaperone and Metabolic pathway.
Silke Leimkühler mostly deals with Biochemistry, Enzyme, Cofactor, Molybdenum cofactor and Aldehyde oxidase. All of her Biochemistry and Amino acid, Biosynthesis, Oxidoreductase, Heme and Succinate dehydrogenase investigations are sub-components of the entire Biochemistry study. Her research integrates issues of Stereochemistry and Metabolism in her study of Enzyme.
While the research belongs to areas of Cofactor, Silke Leimkühler spends her time largely on the problem of Escherichia coli, intersecting her research to questions surrounding Mutant. Her study looks at the intersection of Molybdenum cofactor and topics like Transfer RNA with Molybdopterin. Silke Leimkühler combines subjects such as Furfural, Galactose oxidase, Drug metabolism, Isozyme and Superoxide with her study of Aldehyde oxidase.
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Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus
James J Truglio;Karsten Theis;Silke Leimkühler;Roberto Rappa.
Structure (2002)
Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli.
Chantal Iobbi-Nivol;Silke Leimkühler.
Biochimica et Biophysica Acta (2013)
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.
Journal of Biological Chemistry (2001)
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.
Journal of Biological Chemistry (2001)
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.
Proceedings of the National Academy of Sciences of the United States of America (2004)
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.
Coordination Chemistry Reviews (2011)
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.
Green Chemistry (2015)
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.
FEBS Journal (2013)
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.
Journal of Biological Chemistry (2008)
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.
Molecular Microbiology (1998)
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