| Veranstaltungskalender der Universität Osnabrück >> August 2013 >> | Angemeldet als: Gast |
| Titel: | Prof. Dr. Tony Moore (Brighton): The beauty and the beast of the alternative oxidase: from thermogenic plants to pathogenic parasites |
| Startdatum/-zeit:: | 02.07.2013 17:15 |
| Enddatum/-zeit: | 02.07.2013 19:00 |
| Veranstalter: | |
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| Adresse: | Prof. Dr. Renate Scheibe Koordination: apl. Prof. Dr. Merzendorfer Barbarastr. 11 49076 Osnabrück |
| Telefon: | 0541/969-3502 |
| Telefax: | |
| E-Mail: | merzendorfer@biologie.uni-osnabrueck.de |
| Homepage: | http://www.biologie.uni-osnabrueck.de/Fachbereich/?x=aaad,aczx,gn |
| Veranstaltungsort: | |
| Adresse: | Biologiegebäude, Hörsaal 35/E01 Barbarastr. 11 49076 Osnabrück |
| Beschreibung: | The alternative oxidase is a non-protonmotive respiratory chain protein that catalyses the four electron reduction of oxygen to water. It is ubiquitous amongst the plant kingdom where it has a diverse set of functions from thermogenesis to an oxygen radical scavenger. It is also found in a number of phytopathogenic fungi (including the die-back fungus, Chalara fraxinea) and importantly in parasites such as Trypanosoma brucei, Cryptosporidium parvum and Candida albicans. Trypanosoma brucei is the causative agent of human sleeping sickness and nagana in cattle for which there is currently no effective treatment. The presence of the alternative oxidase allows the parasite to survive in the human bloodstream and since this protein is absent from mammals it is an important therapeutic target. Although the alternative oxidase has been known since the last century little was known about its structure or mechanism of action. We have recently solved the structure of this enigmatic protein and results will be presented as to how such information has allowed us to gain insight into its mechanism of action and direct future rational drug design. The structure reveals that AOX is a dimeric monotopic protein that contains a diiron carboxylate active-site that is buried deep within the hydrophobic environment of a four helix bundle. A comparison with other dicarboxylate proteins such as ribonucleotide reductase has allowed us to formulate models of the plant alternative oxidase and provide information as to how the plant protein is regulated in vivo. |
| Kategorie: | SFB-Seminare (Biologie) |