http://www.imbg-grenoble.fr

Courses, Lectures and Keynotes


Courses:

- F. Barras (LCB, Marseille, France): Genetics and Regulation of Fe-S cluster biogenesis in E. coli.

- G. Blondin (CBM, Grenoble, France) and S. Gambarelli (INAC, LCIB, UJF/CEA , Grenoble, France): EPR and Mössbauer spectroscopies : basic principles and applications to Fe-S clusters.

- S. J. Booker (Department of Chemistry at Penn State, USA): Accurate determination of configuration and stoichiometry of clusters in iron-sulfur proteins.

- C. Drennan (MIT, Cambridge, USA): Structural methods for studying oxygen-sensitive metalloproteins.

- B. M. Hoffman (Northwestern University, Evanston, USA): Advanced paramagnetic resonance spectroscopies : basic principles and applications to Fe-S enzymes.

- F. Meyer (Institut für Anorganische Chemie, Göttingen, Germany): Synthetic approaches to, and reactions of, biomimetic complexes containing iron and sulfur.

- H. Puccio (IGBMC, Strasbourg, France): Human diseases linked to iron-sulfur biogenesis.


Plenary lectures:

- F. Barras (LCB, Marseille, France): The role of Fe-S cluster proteins in antibiotic resistance in E. coli.

- S. J. Booker (Department of Chemistry at Penn State, USA): Radical mechanisms of post-transcriptional and/or post-translational modifications.

- C. Drennan (MIT, Cambridge, USA): Snapshots of AdoMet radical enzymes.

- B. M. Hoffman (Northwestern University, Evanston, USA): Fe-S clusters: Nature’s other all-purpose metallo-cofactor.

- F. Meyer (Institut für Anorganische Chemie, Göttingen, Germany): Proton Coupled Electron Transfer at Biomimetic [2Fe-2S] Clusters.

- H. Puccio (IGBMC, Strasbourg, France): Understanding mammalian iron-sulfur cluster assembly and the pathophysiology of Friedreich ataxia.


Keynotes:

- M. Atta (CEA-UGA, Grenoble, France): S-Adenosylmethionine-dependent radical-based modification of biological macromolecules: Role of the additional iron-sulfur cluster in catalysis.

- S. De Beer (Max-Planck-Institute, Mülheim, Germany): Insights into Biological N2 Reduction: Spectroscopic Studies of the Vanadium and Molybdenum Nitrogenases.

- C. Leger (BIP, Marseille, France): Mechanistic studies of hydrogenases.

- S. Leimkühler (University of Potsdam, Germany): The biosynthesis of the molybdenum cofactor in bacteria.

- A. Magalon (LCB, Marseille, France): A conserved structural motif is involved in molybdenum cofactor insertion.

- T. Matsumoto (University of Nagoya, Japan): Model studies of Acetyl CoA Synthase.

- Y. Nicolet (IBS, Grenoble, France): FeFe-Hydrogenase Assembly Machinery: Structure and Function of the Maturase HydG.

- C. Pickett (University of East Anglia, UK): CO, CN and H Chemistry at 4Fe4S clusters.

- T. Rauchfuss (University of Illinois, USA): Mechanistic Insights into the FeFe- and NiFe-Hydrogenases Through Synthetic Models.

- P. Roach (University of Southampton, UK): Crystal Structure of HydG and [FeFe] Hydrogenase H-Cluster Biosynthesis.

- G. Schwarz (University of Koln, Germany): Molybdenum enzymes in neurodegeneration, drug metabolism and vasodilation.

- K. Tatsumi (Nagoya University, Japan): Chemistry of the Nitrogenase P-Cluster.