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Bioinspired Organometallic Analogues of Iron-Sites in Metalloproteins

Impresion
EUR 39,10

E-Book
EUR 27,00

Bioinspired Organometallic Analogues of Iron-Sites in Metalloproteins (Tienda española)

Steffen Meyer (Autor)

Previo

Indice, PDF (140 KB)
Lectura de prueba, PDF (270 KB)

ISBN-13 (Impresion) 9783954049202
ISBN-13 (E-Book) 9783736949201
Idioma Inglés
Numero de paginas 184
Laminacion de la cubierta mate
Edicion 1. Aufl.
Lugar de publicacion Göttingen
Lugar de la disertacion Göttingen
Fecha de publicacion 29.01.2015
Clasificacion simple Tesis doctoral
Area Química
Palabras claves Bioinorganic Chemistry, Organometallic Chemistry, Iron, Metalloproteins, N-Heterocyclic Carbene, Oxoiron (IV)
Descripcion

Metalloproteins with iron-sites are essential for almost all living organisms and responsible for a large number of biological redox reactions. To uncover the mechanisms of enzymes and cofactors, bioinorganic chemistry aims to provide low-molecular weight analogues. In this dissertation, the iron-sites of [2Fe–2S] proteins, [NiFe] hydrogenases and mononuclear oxygenases served as models for bioinspired analogues coordinated by N-heterocyclic carbene (NHC) ligands. Although abiological, NHC ligands have been shown to be capable of stabilizing otherwise labile inorganic intermediates which are crucial for mechanistic understanding. Using this approach, the isolation of the first organometallic oxoiron(IV) complex, mimicking the oxygenase motif, was achieved. Studies on the structural and magnetic characteristics, substrate reactivity, and the decomposition pathway are provided.