Information for Researchers No. 53 | 29 August 2018
Priority Programme “Iron-Sulfur for Life: Cooperative Function of Iron-Sulfur Centers in Assembly, Biosynthesis, Catalysis and Disease” (SPP 1927)
The Senate of the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) established the Priority Programme “Iron-Sulfur for Life: Cooperative Function of Iron-Sulfur Centers in Assembly, Biosynthesis, Catalysis and Disease” (SPP 1927). The programme is designed to run for six years. The present call invites proposals for the second 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 (Moco) of various molybdoenzymes as well as the active sites of 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, or nickel. These metals are essential constituents for nitrogenase, hydrogenase and selected molybdo/tungstoenzymes. Novel methodological improvements will 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. 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. The following fundamental areas will be addressed:
- assembly of complex FeS proteins as a starting point for versatile functionality
- biosynthesis and crosstalk of complex metal cofactors by FeS proteins
- catalysis and functions of complex FeS proteins
- mechanistic and regulatory roles of FeS proteins in a cellular context
It is anticipated that in the four areas within the programme innovative studies will be supported towards answering key questions on:
- the crosstalk of metals in the assembly and biosynthesis of protein active site metal centers with a focus on the biosynthesis of generic FeS clusters, the molybdenum/tungsten cofactor, the iron-molybdenum cofactor, (NiFe), (FeFe) and (Fe) centers of hydrogenase and nitrogenase-like centers
- novel reactions of binuclear metal clusters in nitrogenase-like enzymes, hydrogenases and molybdoenzymes, the characterisation of “novel” FeS centers in proteins, in addition to “dual-function” activities of proteins in the biosynthesis of metal-cofactors with multiple roles at the cellular level
- metal-binding, assembly and cofactor insertion of complex FeS-containing enzymes by the identification of the involved proteins
- studies on metal homeostasis and transfer of FeS clusters at a cellular level
- novel spectroscopic developments to study FeS-related proteins at a cellular level
It is expected that successful applications will propose visionary work on FeS center biogenesis, cofactor insertion, and catalytic function, with the focus on studying complex FeS cluster-containing proteins (hydrogenase, nitrogenase, molybdoenzymes). Ideally, the successful projects cover at least two of the four fundamental areas. Collaborative studies across the four areas are crucial for integration into the Priority Programme, and project proposals covering only one area will not be considered.
The following research questions are excluded:
- studies on well-established metal centers involved in photosynthesis, respiratory chains or oxygenases, e.g., heme-containing enzymes
- studies on FeS-containing enzymes where the clusters have solely a structural role
- studies on medical iron-related diseases that solely study iron transport and do not directly address the biosynthesis of metal clusters or the activity of metal-cofactor containing enzymes
- studies on isolated, mono-functional FeS-containing enzymes that do not provide a cross-talk to other cofactor systems
- FeS-cluster-independent enzyme-systems containing metals other than Mo, W, Ni, Fe
Proposals must be written in English and submitted to the DFG by 29 January 2019. Please note that proposals can only be submitted via elan, the DFG’s electronic proposal processing system. If you would like to submit a proposal for a new project within the existing Priority Programme, please go to Proposal Submission – New Project – Priority Programmes and select “SPP 1927” from the current list of calls. Previous applicants can submit a proposal for the renewal of an existing project under Proposal Submission – Proposal Overview/Renewal Proposal.
In preparing your proposal, please review the programme guidelines (form 50.05, section B) and follow the proposal preparation instructions (form 54.01). These forms can either be downloaded from our website or accessed through the elan portal.
Applicants must be registered in elan prior to submitting a proposal to the DFG. If you have not yet registered, please note that you must do so by 15 January 2019 to submit a proposal under this call; registration requests received after this time cannot be considered. You will normally receive confirmation of your registration by the next working day. Note that you will be asked to select the appropriate Priority Programme call during both the registration and the proposal process.
The review will be held during a proposal colloquium scheduled to take place in Potsdam in April 2019.
More information on the Priority Programme is available under:
The elan system can be accessed at:
DFG forms 50.05 and 54.01 can be downloaded at:
For scientific enquiries please contact the coordinator of the Priority Programme:
- Prof. Dr. Silke Leimkühler,
Institut für Biochemie und Biologie,
phone +49 331 977-5603,
Link auf E-Mailsleim@uni-potsdam.de
Questions on the DFG proposal process can be directed to:
- Programme contact:
phone +49 228 885-2441,
Link auf E-Mailnikolai.email@example.com
- Administrative contact:
phone +49 228 885-2249,
Link auf E-Mailsylvia.firstname.lastname@example.org
This text is available at Interner Linkwww.dfg.de/foerderung/info_wissenschaft/2018/info_wissenschaft_18_53. Please use this identifier to cite or link to this item.