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Silke Leimkühler (1970-)

Biologin

Name	Silke Leimkühler
Zeit	1970- (Lebensdaten)
Ort	Deutschland
Akademischer Grad bzw. Titel	Prof. Dr.
Beruf	Biologin (charakteristischer Beruf)
Variante	S. Leimkühler
Beziehung	Universität Potsdam
Weitere Angaben	Habil. Lehrgebiete Biochemie und Mikrobiologie, Techn. Univ. Braunschweig, 2005 seit 2009 Professorin für Molekulare Enzymologie an der Universität Potsdam
Datensatztyp	Person
GND-Nummer	130441422
Datensatz-ID	130441422
Beteiligt an alle anzeigen Coupling of the Catalytic Reactions of Formate Dehydrogenase and Hydrogenase in Solution: Insights from in situ IR Spectroscopy and Computations Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL A Minimal Light‐Driven System to Study the Enzymatic CO2 Reduction of Formate Dehydrogenase Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL Dissecting the role of the TusA protein for cell functionality and FtsZ ring assembly in Escherichia coli Molybdenum homeostasis in fungi and the necessity for dietary molybdenum cofactor in nematodes Role of the tRNA thiouridine modification protein (TUM1) as a sulfurtransferase in humans The Human Mercaptopyruvate Sulfurtransferase TUM1 Is Involved in Moco Biosynthesis, Cytosolic tRNA Thiolation and Cellular Bioenergetics in Human Embryonic Kidney Cells The Mechanism of Metal-Containing Formate Dehydrogenases Revisited: The Formation of Bicarbonate as Product Intermediate Provides Evidence for an Oxygen Atom Transfer Mechanism A Minimal Light‐Driven System to Study the Enzymatic CO 2 Reduction of Formate Dehydrogenase Infrared Spectroscopy Elucidates the Inhibitor Binding Sites in a Metal‐Dependent Formate Dehydrogenase Infrared spectroscopy elucidates the inhibitor binding sites in a metal-dependent formate dehydrogenase Infrared spectroscopy elucidates the inhibitor binding sites in a metal-dependent formate dehydrogenase ROS Generation in Human Aldehyde Oxidase And the Effects of ROS and Reactive Sulfhydryl on the Activity of the Enzyme A-Type Carrier Proteins are involved in [4Fe-4S] Cluster insertion into the Radical S-adenosylmethionine (SAM) Protein MoaA and other molybdoenzymes Reconstitution of molybdenum cofactor biosynthesis in giant vesicles From single molecules to bulk materials: tuning the viscoelastic properties of coiled coil cross-linked hydrogels The biosynthesis of the molybdenum cofactors in Escherichia coli The 1,6,7,12‐Tetraazaperylene Bridging Ligand as an Electron Reservoir and Its Disulfonato Derivative as Redox Mediator in an Enzyme–Electrode Process Cover Feature: The 1,6,7,12‐Tetraazaperylene Bridging Ligand as an Electron Reservoir and Its Disulfonato Derivative as Redox Mediator in an Enzyme–Electrode Process (Chem. Eur. J. 62/2017) Molybdenum and sulfur in biological systems : characterization of molybdoenzymes and the pathway for the biosynthesis of the molybdenum cofactor in bacteria and humans

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Katalog der Deutschen Nationalbibliothek

Silke Leimkühler (1970-)

Coupling of the Catalytic Reactions of Formate Dehydrogenase and Hydrogenase in Solution: Insights from in situ IR Spectroscopy and Computations

Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL

Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL

A Minimal Light‐Driven System to Study the Enzymatic CO2 Reduction of Formate Dehydrogenase

Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL

Discovery of the Lanthipeptide Curvocidin and Structural Insights into its Trifunctional Synthetase CuvL

Dissecting the role of the TusA protein for cell functionality and FtsZ ring assembly in Escherichia coli

Molybdenum homeostasis in fungi and the necessity for dietary molybdenum cofactor in nematodes

Role of the tRNA thiouridine modification protein (TUM1) as a sulfurtransferase in humans

The Human Mercaptopyruvate Sulfurtransferase TUM1 Is Involved in Moco Biosynthesis, Cytosolic tRNA Thiolation and Cellular Bioenergetics in Human Embryonic Kidney Cells

The Mechanism of Metal-Containing Formate Dehydrogenases Revisited: The Formation of Bicarbonate as Product Intermediate Provides Evidence for an Oxygen Atom Transfer Mechanism

A Minimal Light‐Driven System to Study the Enzymatic CO 2 Reduction of Formate Dehydrogenase

Infrared Spectroscopy Elucidates the Inhibitor Binding Sites in a Metal‐Dependent Formate Dehydrogenase

Infrared spectroscopy elucidates the inhibitor binding sites in a metal-dependent formate dehydrogenase

Infrared spectroscopy elucidates the inhibitor binding sites in a metal-dependent formate dehydrogenase

ROS Generation in Human Aldehyde Oxidase And the Effects of ROS and Reactive Sulfhydryl on the Activity of the Enzyme

A-Type Carrier Proteins are involved in [4Fe-4S] Cluster insertion into the Radical S-adenosylmethionine (SAM) Protein MoaA and other molybdoenzymes

Reconstitution of molybdenum cofactor biosynthesis in giant vesicles

From single molecules to bulk materials: tuning the viscoelastic properties of coiled coil cross-linked hydrogels

The biosynthesis of the molybdenum cofactors in Escherichia coli

The 1,6,7,12‐Tetraazaperylene Bridging Ligand as an Electron Reservoir and Its Disulfonato Derivative as Redox Mediator in an Enzyme–Electrode Process

Cover Feature: The 1,6,7,12‐Tetraazaperylene Bridging Ligand as an Electron Reservoir and Its Disulfonato Derivative as Redox Mediator in an Enzyme–Electrode Process (Chem. Eur. J. 62/2017)

Molybdenum and sulfur in biological systems : characterization of molybdoenzymes and the pathway for the biosynthesis of the molybdenum cofactor in bacteria and humans