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Priority Programme Iron-Sulfur for Life: Cooperative Function of Iron-Sulfur Centers in Assembly, Biosynthesis, Catalysis and Disease (SPP 1927)
Termin:
30.09.2015
Fördergeber:
Deutsche Forschungsgemeinschaft (DFG)
The Senate of the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) has decided to establish a Priority Programme, entitled Iron-Sulfur for Life: Cooperative Function of Iron-Sulfur Centers in Assembly, Biosynthesis, Catalysis and Disease . The programme will commence in 2016 and is designed to run for six years. Applications are now invited for the first three-year funding period.
Iron-sulfur (FeS) centers are essential protein cofactors in all forms of life. In particular, FeS centers function as enzyme cofactors in catalysis and electron transfer. Moreover, they are indispensable for the biosynthesis of complex metal centers such as the iron-molybdenum cofactor (FeMoco) of nitrogenase, the molybdenum cofactor of various molybdoenzymes as well as the active sites of [FeFe]- and [Fe]-hydrogenases. In spite of recent fundamental breakthroughs in metalloenzyme research, it has become evident that studies on single enzymes need to be transformed into the broader context of a living cell where biosynthesis, function, and assembly/disassembly of these fascinating metal cofactors are coupled in a dynamic fashion. Various biosynthetic pathways were found to be tightly interconnected through complex crosstalk mechanisms that crucially depend on the bio-availability of the metal ions iron, molybdenum, tungsten, nickel, copper, and zinc. These metals are essential constituents for nitrogenase, hydrogenase and selected molybdo-/tungstoenzymes. Novel methodological developments shall allow for a detailed investigation of the biosynthesis and catalytic function of FeS-dependent enzymes in a cellular context, thus, opening up a new era in metalloenzyme studies. Moreover, cellular studies are a prerequisite for obtaining a comprehensive view on the involvement of metalloenzymes in metal-related human diseases. Further, the programme aims at the development of future cellular systems for bioenergy production, fertilisation and bio-applications. In order to adequately address these questions, novel, interdisciplinary concepts and approaches shall be combined with novel technological advancements.
Understanding the crosstalk of metal ions on a cellular basis requires multidisciplinary and cooperative approaches that span the entire range from cell and molecular biology, biochemistry, inorganic chemistry, spectroscopy, and structural biology to theory. In the Priority Programme it is planned to study novel enzyme mechanisms, innovative model complexes, and to define the mechanistic basis of the metal center biogenesis pathways in the (patho-)physiological context of living organisms.
For scientific enquiries please contact the coordinator of the Priority Programme:
Prof. Dr. Silke Leimkühler, Institut für Biochemie und Biologie, Universität Potsdam, Karl-Liebknecht-Str. 24 25, 14476 Potsdam, phone +49 331 977-5603, sleim@uni-potsdam.de
For administrative enquiries please contact:
Dr. Nikolai Raffler, phone +49 228 885-2441, nikolai.raffler@dfg.de
Franziska Wunschik, phone +49 228 885-2622, franziska.wunschik@dfg.de
Further Information:
http://www.dfg.de/foerderung/info_wissenschaft/info_wissenschaft_15_45/index.html
Iron-sulfur (FeS) centers are essential protein cofactors in all forms of life. In particular, FeS centers function as enzyme cofactors in catalysis and electron transfer. Moreover, they are indispensable for the biosynthesis of complex metal centers such as the iron-molybdenum cofactor (FeMoco) of nitrogenase, the molybdenum cofactor of various molybdoenzymes as well as the active sites of [FeFe]- and [Fe]-hydrogenases. In spite of recent fundamental breakthroughs in metalloenzyme research, it has become evident that studies on single enzymes need to be transformed into the broader context of a living cell where biosynthesis, function, and assembly/disassembly of these fascinating metal cofactors are coupled in a dynamic fashion. Various biosynthetic pathways were found to be tightly interconnected through complex crosstalk mechanisms that crucially depend on the bio-availability of the metal ions iron, molybdenum, tungsten, nickel, copper, and zinc. These metals are essential constituents for nitrogenase, hydrogenase and selected molybdo-/tungstoenzymes. Novel methodological developments shall allow for a detailed investigation of the biosynthesis and catalytic function of FeS-dependent enzymes in a cellular context, thus, opening up a new era in metalloenzyme studies. Moreover, cellular studies are a prerequisite for obtaining a comprehensive view on the involvement of metalloenzymes in metal-related human diseases. Further, the programme aims at the development of future cellular systems for bioenergy production, fertilisation and bio-applications. In order to adequately address these questions, novel, interdisciplinary concepts and approaches shall be combined with novel technological advancements.
Understanding the crosstalk of metal ions on a cellular basis requires multidisciplinary and cooperative approaches that span the entire range from cell and molecular biology, biochemistry, inorganic chemistry, spectroscopy, and structural biology to theory. In the Priority Programme it is planned to study novel enzyme mechanisms, innovative model complexes, and to define the mechanistic basis of the metal center biogenesis pathways in the (patho-)physiological context of living organisms.
For scientific enquiries please contact the coordinator of the Priority Programme:
Prof. Dr. Silke Leimkühler, Institut für Biochemie und Biologie, Universität Potsdam, Karl-Liebknecht-Str. 24 25, 14476 Potsdam, phone +49 331 977-5603, sleim@uni-potsdam.de
For administrative enquiries please contact:
Dr. Nikolai Raffler, phone +49 228 885-2441, nikolai.raffler@dfg.de
Franziska Wunschik, phone +49 228 885-2622, franziska.wunschik@dfg.de
Further Information:
http://www.dfg.de/foerderung/info_wissenschaft/info_wissenschaft_15_45/index.html