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Multiple Rieske proteins in prokaryotes: where and why?
Dirk Schneider1, Christian L Schmidt
1Albert-Ludwigs-University Freiburg, Institut für Biochemie und Molekularbiologie, Stefan-Meier-Strasse 19, 79104 Freiburg, Germany. Dirk.Schneider@biochemie.uni-freiburg.de
Biochimica Et Biophysica Acta
|November 8, 2005
Summary
Multiple high potential Rieske proteins in prokaryotes are key for adapting electron transfer chains. This adaptation allows microbes to better respond to changing environmental conditions.
Area of Science:
- Microbiology
- Biochemistry
- Genomics
Background:
- Rieske iron-sulfur proteins are essential subunits of cytochrome bc-type complexes and oxygenases.
- Multiple genes encoding these proteins are found in diverse prokaryotic and eukaryotic genomes.
- The function of multiple high potential Rieske proteins in cytochrome bc-type complexes remains largely unknown.
Purpose of the Study:
- To summarize recent findings on the characteristics and physiological functions of multiple high potential Rieske proteins in prokaryotes.
- To explore the adaptive significance of these proteins in microbial electron transfer chains.
Main Methods:
- Literature review of recent studies on Rieske proteins in prokaryotes.
- Analysis of genomic data and functional investigations.
Main Results:
- The diversity of low potential Rieske proteins linked to oxygenases is explained by varied substrates and reactions.
- The physiological roles of multiple high potential Rieske proteins in cytochrome bc-type complexes are still under investigation.
- Initial studies suggest these proteins play a role in adapting electron transfer chains.
Conclusions:
- Multiple high potential Rieske proteins in prokaryotes likely contribute to adapting electron transfer chains.
- This adaptability may be crucial for microbial survival under changing environmental conditions.