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              Printable Handouts
Navigable Slide Index
- Introduction
 - Talk outline
 - Diverse structures of Fe/S clusters
 - Coordination of Fe/S clusters
 - Functions of Fe/S clusters: electron transfer
 - Functions of Fe/S clusters: catalysis, regulation
 - Functions of Fe/S clusters: S donor, stabilization
 - How do we study Fe/S proteins in vitro?
 - How do we study Fe/S proteins in vivo? (1)
 - How do we study Fe/S proteins in vivo? (2)
 - Active maturation of eukaryotic Fe/S proteins
 - First model for cellular Fe/S protein biogenesis
 - Biogenesis of cellular Fe/S proteins
 - Biogenesis of mitochondrial Fe/S proteins I
 - De novo Fe/S cluster assembly
 - Structural glimpse: Human core Isc complex
 - Biogenesis of mitochondrial Fe/S proteins II, III
 - Mitochondrial Fe/S proteins biogenesis in yeast
 - Mitochondrial Fe/S proteins biogenesis in man
 - Multiple mitochondrial dysfunctions syndromes
 - Conclusions and open questions
 - Acknowledgments
 
Topics Covered
- Structure and functions of iron-sulfur (Fe/S) clusters and proteins
 - Analysis of Fe/S proteins and their biogenesis
 - Mechanisms of Fe/S protein assembly in mitochondria
 - Mitochondrial “Fe/S diseases“
 
Links
Series:
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Talk Citation
Lill, R. (2018, March 29). Biogenesis of cellular iron-sulfur proteins: structure, function, and assembly in mitochondria [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 4, 2025, from https://doi.org/10.69645/OTWE7345.Export Citation (RIS)
Publication History
- Published on March 29, 2018
 
Financial Disclosures
- Prof. Roland Lill has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
 
Biogenesis of cellular iron-sulfur proteins: structure, function, and assembly in mitochondria
                  Published on March 29, 2018
                  
                    
                      
                        
                      
                    
                  
                  
                    49 min
                
              Other Talks in the Series: Mitochondria in Health and Disease
Transcript
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                  0:00
                
                
                  
                    Hello, my name is Roland Lill,
                  
                    I'm a Professor of Cell Biology at
                  
                    the Institute of Zytobiologie at the Philipps- Universitat of Marburg, in Germany.
                  
                    In my lecture, I will try to give you an overview on what we learned over
                  
                    the past two decades on the Biogenesis of Cellular Iron-Sulfur Proteins in Eukaryotes.
                  
                
              
                  0:23
                
                
                  
                    In part one of my lecture,
                  
                    I will first provide you with a general overview on
                  
                    the structure and function of Iron-Sulfur clusters and proteins in nature.
                  
                    Then I will briefly introduce you into
                  
                    the biochemical and spectroscopic methods of how
                  
                    we can analyze Iron-Sulfur proteins and their biogenesis.
                  
                    Next, I will concentrate on what we know about
                  
                    the mechanisms of the Iron-Sulfur protein assembly in mitochondria.
                  
                    This is then followed by a brief overview of
                  
                    the so-called mitochondrial Iron-Sulfur diseases.
                  
                    And finally, I will discuss a few open questions in this exciting research field.
                  
                    In part two, I will cover the role of mitochondrion and assembly.
                  
                    I will talk on cytosolic and nuclear Iron-Sulfur proteins,
                  
                    the mechanisms of this process and about a number of
                  
                    essential cellular processes intimately connected
                  
                    to cytosolic and nuclear Iron-Sulfur protein biogenesis.
                  
                
              
                  1:28
                
                
                  
                    Iron-Sulfur clusters are among the oldest and most simple protein co-factors we know.
                  
                    The simplest form of Iron-Sulfur clusters are
                  
                    the rhombic 2Fe-2S clusters on the left,
                  
                    and the cubic 4Fe-4S cluster on the right.
                  
                    Together, they comprise more than 90% of the clusters we know, in the living world.
                  
                    The clusters are usually coordinated by
                  
                    the iron-ions to cysteine residues of the polypeptide chain.
                  
                    However, we know other forms of Iron-Sulfur clusters such
                  
                    as the 3Fe-4S or 4Fe-3S clusters,
                  
                    where simply a 4Fe-4S cluster has lost either an iron or a sulfur-iron respectively,
                  
                    for instance, in the latter case in oxygen resistant hydrogenase.
                  
                    More complex Iron-Sulfur clusters are present for instance in the well
                  
                    studied bacterial protein nitrogenase, which exists nitrogen.
                  
                    Its P-cluster on the left is comprised of two 4Fe-4S clusters fused via a sulfur atom.
                  
                    In the M or molybdenum cluster on the right,
                  
                    one of the iron ions is replaced by another metal,
                  
                    in this case molybdenum but can also be
                  
                    vanadium giving rise to a rather complex cluster structure.
                  
                
              
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