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Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands

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Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands (Tienda española)

Model Studies Using Synthetic Analogues

Marie Bergner (Autor)


Indice, PDF (120 KB)
Lectura de prueba, PDF (440 KB)

ISBN-13 (Impresion) 9783736996724
ISBN-13 (E-Book) 9783736986725
Idioma Inglés
Numero de paginas 198
Laminacion de la cubierta mate
Edicion 1.
Lugar de publicacion Göttingen
Lugar de la disertacion Göttingen
Fecha de publicacion 07.12.2017
Clasificacion simple Tesis doctoral
Area Química
Palabras claves bioinorganic chemistry, iron-sulfur clusters, [2Fe-2S], model compounds, ligand rearrangement, mitoNEET, proton coupled electron transfer, electrochemistry

Iron sulfur clusters are essential cofactors involved in electron transfer, sensing, and catalysis in all three kingdoms of life. While most iron sulfur clusters are ligated by cysteine thiolates, a number of clusters featuring so called alternative ligands such as histidine have been recognized in recent years. This work uses synthetic [2Fe-2S] analogues to explore the role alternative ligands play in determining the reactivity of iron sulfur clusters. Isomerization in a homoleptically coordinated cluster utilizing a mixed nitrogen- and sulfur-donating ligand is investigated as a model for ligand rearrangement processes during iron sulfur cluster biogenesis. Furthermore, a high fidelity model system for the asymmetrically ligated [2Fe-2S] cluster of mitoNEET proteins is developed and characterized in detail. This cluster and its homoleptic analogue are studied as reagents in proton coupled electron transfer processes, highlighting the role asymmetry and reorganization energy play in tuning this reactivity. The effects of the ligation pattern on entropic contributions during reduction are probed by temperature dependent electrochemical measurements. Finally, synthetic [2Fe-2S] clusters are investigated with respect to their reactivity with organic radicals, mimicking the unique reactivity of biotin synthase.