![A Minimal Light‐Driven System to Study the Enzymatic CO2 Reduction of Formate Dehydrogenase - Laun - 2022 - ChemCatChem - Wiley Online Library A Minimal Light‐Driven System to Study the Enzymatic CO2 Reduction of Formate Dehydrogenase - Laun - 2022 - ChemCatChem - Wiley Online Library](https://chemistry-europe.onlinelibrary.wiley.com/cms/asset/8308eb81-b6cb-4f5e-944e-d86ec5a4c898/cctc202201067-toc-0001-m.jpg)
A Minimal Light‐Driven System to Study the Enzymatic CO2 Reduction of Formate Dehydrogenase - Laun - 2022 - ChemCatChem - Wiley Online Library
![Amazon.com: Transition Metals in Catalysis: The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems: 9783036506081: Leimkühler, Silke, Magalon, Axel, Einsle, Oliver Amazon.com: Transition Metals in Catalysis: The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems: 9783036506081: Leimkühler, Silke, Magalon, Axel, Einsle, Oliver](https://m.media-amazon.com/images/I/61ApZ8qhCQL._AC_UF1000,1000_QL80_.jpg)
Amazon.com: Transition Metals in Catalysis: The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems: 9783036506081: Leimkühler, Silke, Magalon, Axel, Einsle, Oliver
![Anion Binding and Oxidative Modification at the Molybdenum Cofactor of Formate Dehydrogenase from Rhodobacter capsulatus Studied by X-ray Absorption Spectroscopy • Wissenschaftliches Rechnen • Freie Universität Berlin Anion Binding and Oxidative Modification at the Molybdenum Cofactor of Formate Dehydrogenase from Rhodobacter capsulatus Studied by X-ray Absorption Spectroscopy • Wissenschaftliches Rechnen • Freie Universität Berlin](https://www.fu-berlin.de/sites/high-performance-computing/Forschungsergebnisse/_ressourcen/Duffus2019_10_1021_2Facs_inorgchem_9b01613.png?width=350)
Anion Binding and Oxidative Modification at the Molybdenum Cofactor of Formate Dehydrogenase from Rhodobacter capsulatus Studied by X-ray Absorption Spectroscopy • Wissenschaftliches Rechnen • Freie Universität Berlin
![The biosynthesis of the molybdenum cofactors in Escherichia coli - Leimkühler - 2020 - Environmental Microbiology - Wiley Online Library The biosynthesis of the molybdenum cofactors in Escherichia coli - Leimkühler - 2020 - Environmental Microbiology - Wiley Online Library](https://ami-journals.onlinelibrary.wiley.com/cms/asset/d7f5efcb-6b39-4a9e-9223-2024c318079b/emi.v22.6.cover.jpg?trick=1691973321689)
The biosynthesis of the molybdenum cofactors in Escherichia coli - Leimkühler - 2020 - Environmental Microbiology - Wiley Online Library
![allweknow about Catalysis - Prof. Dr. Leimkühler & Prof. Dr. Roldan Cuenya - UniSysCat/TU Berlin - YouTube allweknow about Catalysis - Prof. Dr. Leimkühler & Prof. Dr. Roldan Cuenya - UniSysCat/TU Berlin - YouTube](https://i.ytimg.com/vi/3hqI4FFfh68/sddefault.jpg)
allweknow about Catalysis - Prof. Dr. Leimkühler & Prof. Dr. Roldan Cuenya - UniSysCat/TU Berlin - YouTube
Infrared spectroscopy elucidates the inhibitor binding sites in a metal-dependent formate dehydrogenase
![PDF] The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form by Fabio Forlani, Angelo Cereda, Andrea Freuer, Manfred Nimtz, Silke Leimkühler, Silvia Pagani · 10.1016/j.febslet.2005.11.013 · OA.mg PDF] The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form by Fabio Forlani, Angelo Cereda, Andrea Freuer, Manfred Nimtz, Silke Leimkühler, Silvia Pagani · 10.1016/j.febslet.2005.11.013 · OA.mg](https://og.oa.mg/The%20cysteine-desulfurase%20IscS%20promotes%20the%20production%20of%20the%20rhodanese%20RhdA%20in%20the%20persulfurated%20form.png?author=%20Fabio%20Forlani,%20Angelo%20Cereda,%20Andrea%20Freuer,%20Manfred%20Nimtz,%20Silke%20Leimk%C3%BChler,%20Silvia%20Pagani)
PDF] The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form by Fabio Forlani, Angelo Cereda, Andrea Freuer, Manfred Nimtz, Silke Leimkühler, Silvia Pagani · 10.1016/j.febslet.2005.11.013 · OA.mg
![Nature Communications on X: "The labs of Petra Wendler & Silke Leimkühler @unipotsdam and their collaborators solved the cryo-EM structure of the molybdoenzyme formate dehydrogenase https://t.co/wPBFOcARSP https://t.co/mr8jIaf8I3" / X Nature Communications on X: "The labs of Petra Wendler & Silke Leimkühler @unipotsdam and their collaborators solved the cryo-EM structure of the molybdoenzyme formate dehydrogenase https://t.co/wPBFOcARSP https://t.co/mr8jIaf8I3" / X](https://pbs.twimg.com/media/EWWudx0XYAA2STx.png)
Nature Communications on X: "The labs of Petra Wendler & Silke Leimkühler @unipotsdam and their collaborators solved the cryo-EM structure of the molybdoenzyme formate dehydrogenase https://t.co/wPBFOcARSP https://t.co/mr8jIaf8I3" / X
![PDF) Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer PDF) Electrocatalytic sulfite biosensor with human sulfite oxidase co-immobilized with cytochrome c in a polyelectrolyte-containing multilayer](https://i1.rgstatic.net/publication/23395615_Electrocatalytic_sulfite_biosensor_with_human_sulfite_oxidase_co-immobilized_with_cytochrome_c_in_a_polyelectrolyte-containing_multilayer/links/02bfe5138e4f7651d8000000/largepreview.png)