|
RUN >
Instituto de Tecnologia Química e Biológica (ITQB) >
ITQB R&D Units >
ITQB: Biological Chemistry >
ITQB: Metalloenzymes and Molecular Bioenergetics >
ITQB: MMB - PhD Theses >
Please use this identifier to cite or link to this item:
http://hdl.handle.net/10362/5159
|
| Title: | The alternative complex III from Rhodothermus marinus - a prototype of a new family of quinol: electron acceptor oxidoreductase |
| Authors: | Refojo, Patrícia N. |
| Advisor: | Teixeira, Miguel Pereira, Manuela M. |
| Issue Date: | Jul-2010 |
| Publisher: | Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa |
| Abstract: | The aim of the work presented in this thesis was the characterization of a complex with quinol: electron carrier oxidodoreductase activity present in the membranes of the thermohalophilic bacterium Rhodothermus (R.) marinus.
The complexes involved in the R. marinus respiratory chain have been extensively studied in the past few years. Specifically, the purification and characterization of a complex I (NADH: quinone oxidoreductase), a
complex II (succinate:quinone oxidoreductase) and of three different
oxygen reductases from the heme-copper oxygen reductases superfamily have been performed. Since those oxygen reductases are unable to receive electrons from quinol molecules, the presence of a complex linking complexes I and II to the oxygen reductases was needed. In fact, a complex with quinol: HiPIP oxidoreductase activity was purified and partially characterized. The absence of the Rieske protein indicated that the complex isolated from R. marinus has a different composition when compared with the typical cytochrome bc1 complex.(...) |
| Description: | Dissertation presented to obtain a PhD degree in Biochemistry at the Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa |
| URI: | http://hdl.handle.net/10362/5159 |
| Appears in Collections: | ITQB: MMB - PhD Theses ITQB: BET - PhD Theses
|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.
|