Regensburg 2007 – scientific programme
Parts | Days | Selection | Search | Downloads | Help
BP: Fachverband Biologische Physik
BP 16: Poster Session I
BP 16.52: Poster
Tuesday, March 27, 2007, 17:00–19:30, Poster D
Time-Resolved Spectroscopy on 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 streak camera setup. The work will also resolve structure-function relationships of the FAD binding site during catalysis and at different states of reduction.
We are presenting first results from pure FAD in solution and the FAD cofactor of two structurally similar molybdo iron-sulfur flavoproteins, which are the [CuSMoO2] CO dehydrogenase from Oligotropha carboxidovorans and the [MoSO2] xanthine oxidase from bovine milk.