English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Ligand Rearrangements at Fe/S Cofactors: Slow Isomerization of a Biomimetic [2Fe‐2S] Cluster

MPS-Authors
/persons/resource/persons237849

Roy,  Lisa
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons216825

Neese,  Frank
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons216845

Ye,  Shengfa
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Bergner, M., Roy, L., Dechert, S., Neese, F., Ye, S., & Meyer, F. (2017). Ligand Rearrangements at Fe/S Cofactors: Slow Isomerization of a Biomimetic [2Fe‐2S] Cluster. Angewandte Chemie International Edition, 56(17), 4882-4886. doi:10.1002/anie.201612621.


Cite as: http://hdl.handle.net/21.11116/0000-0007-6F1D-E
Abstract
Ligand exchange plays an important role in the biogenesis of Fe/S clusters, most prominently during cluster transfer from a scaffold protein to its target protein. Although in vivo and in vitro studies have provided some insight into this process, the microscopic details of the ligand exchange steps are mostly unknown. In this work, the kinetics of the ligand rearrangement in a biomimetic [2Fe‐2S] cluster with mixed S/N capping ligands have been studied. Two geometrical isomers of the cluster are present in solution, and mechanistic insight into the isomerization process was obtained by variable‐temperature 1H NMR spectroscopy. Combined experimental and computational results reveal that this is an associative process that involves the coordination of a solvent molecule to one of the ferric ions. The cluster isomerizes at least two orders of magnitude faster in its protonated and mixed‐valent states. These findings may contribute to a deeper understanding of cluster transfer and sensing processes occurring in Fe/S cluster biogenesis.