Projekt

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Iron sulfur [FeS] clusters are highly efficient redox centers that are widely and effectively used by natural metalloproteins in biological redox-reactions. Due to their electrochemical properties, including a finely tunable redox-potential, [FeS]-clusters have a great potential for applied science, including the constitution of defined electron transfer pathways and catalytic redox centers. However, [FeS]-clusters have not been successfully reconstituted within biomolecular building blocks of bio-derived or semi-synthetic materials such as aptazymes or DNA origami-elements. The collaboration between the Happe and the Willner group unites the required expertise in the complementary fields of metalloprotein-research and nucleoapzyme design to tackle this challenging task. They will follow three approaches to realize [4Fe4S]-cluster reconstitution in different types of DNA-scaffolds (aptamer-based, G-quadruplex-based and rigid polygonal DNA-building blocks). After thorough spectroscopic verification of cluster synthesis they will reconstitute two types of catalytic redox systems, the electron relay of sulfite-/nitrite-reductase and the H2-producing H-cluster of [FeFe]-hydrogenases.

• Prof. Dr. Thomas Happe

  Universität Bochum
  Fakultät für Biologie und Biotechnologie
  Lehrstuhl Biochemie der Pflanzen
  AG Photobiotechnologie
  Bochum
  

• Prof. Itamar Willner, Ph.D.

  The Hebrew University of Jerusalem
  Institute of Chemistry
  Department of Organic Chemistry
  Jerusalem
  Israel
  

• Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases

• A safety cap protects hydrogenase from oxygen attack.

• The roles of long-range proton-coupled electron transfer in the directionality and efficiency of [FeFe]-hydrogenases.

• Modelling Photosynthesis with ZnII -Protoporphyrin All-DNA G-Quadruplex/Aptamer Scaffolds.

• Artificial Photosynthesis with Electron Acceptor/Photosensitizer-Aptamer Conjugates.