Darstellung und Charakterisierung von Kofaktoren des Elektronentransfers in artifizieller und nativer Proteinumgebung

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The protein Myoglobin was used as matix-molecule to produce monomeric porphyrins in solution. The protein complexes of differen zinc pheophorbides and zinc protoporphyrin have been studied by UV/Vis and NMR spectroscopy. The protein stability versus unfolding and NMR results Based on quantum mechanical calculations analysis of EPR- and ENDOR-spectra of the light excited triplet state yielded identification of α-protons and methyl β-protons have been identified for the first time. The data acquired agrees well with previously published data on native reaction centers. The terminal electron acceptors, [4Fe4S] centers FA and FB in Photosystem I (PSI), have been modelled by peptides with 16 amino acid length synthezied by SPPS Fmoc strategy. Both peptides incorporated a [4Fe4S] cluster in oxidation state 2 /1 as prooven by UV/Vis, EPR and Mössbauer spectroscopy. The redoxpotential for the one electron reduction was found to be -470 mV for both modell peptides.
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Dokumententyp:
Wissenschaftliche Abschlussarbeiten » Dissertation
Fakultät / Institut:
Fakultät für Chemie
Dewey Dezimal-Klassifikation:
500 Naturwissenschaften und Mathematik » 540 Chemie
Stichwörter:
chlorophyll a, iron-sulfur center, FeS center, Myoglobin, PSI, Photosystem I, solid phase peptide synthesis, SPPS
Beitragende:
Prof. Dr. Gärtner, Wolfgang [Betreuer(in), Doktorvater]
Prof. Dr. rer. nat. Veeman, Wiebren S. [Gutachter(in), Rezensent(in)]
Sprache:
Deutsch
Kollektion / Status:
Dissertationen / Dokument veröffentlicht
Datum der Promotion:
31.05.2006
Dokument erstellt am:
31.05.2006
Dateien geändert am:
18.10.2006
Medientyp:
Text