Darmstadt 2008 – wissenschaftliches Programm
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MO: Fachverband Molekülphysik
MO 16: Biomoleküle
MO 16.7: Poster
Dienstag, 11. März 2008, 14:00–19:00, Poster C1
Time-Resolved Spectroscopy on Molybdo Iron-Sulfur Flavoproteins — •Florian Spreitler1, Astrid Pelzmann2, Ortwin Meyer2, and Jürgen Köhler1 — 1Experimentalphysik IV and BIMF, Universität Bayreuth, Universitätsstraße 30, 95447 Bayreuth, Germany — 2Mikrobiologie, Universität Bayreuth, Universitätsstraße 30, 95447 Bayreuth, Germany
Flavoproteins are of great importance in nature because they function in several life-sustaining processes, such as cellular respiration, redox biochemistry, purine metabolism and the oxidation of CO. Their common cofactor flavin adenine dinocleotide (FAD), which can be bound in a covalent or non-covalent fashion, is thought to be fine-tuned by the respective protein matrix both in its redox properties and the exposure of certain atoms to the solvent.
Our main objective is to study the fast photophysics of FAD in different enzymes and enzyme mutants on timescales between 1 ps and 10 ns using a versatile streak camera setup. The work will also resolve structure-function relationships of the FAD binding site during catalysis and at different states of reduction.
Here, we present time-resolved fluorescence spectra of the FAD cofactor in three structurally similar molybdo iron-sulfur flavoproteins, which are the [CuSMoO2] CO dehydrogenase from Oligotropha carboxidovorans, the [MoSO2] xanthine dehydrogenase from chicken liver and the [MoSO2] xanthine oxidase from bovine milk.