Abstract
The previously detected Rieske iron-sulfur protein from the membranes of the thermoacidophile Sulfolobus acidocaldarius [Anemüller, S., et al. (1993) FEBS Lett. 318, 61-64] was purified to electrophoretic homogeneity and the N-terminal amino acids determined. The apparent molecular weight was estimated to be 32 kDa. The reduced protein displays a rhombic EPR spectrum with gxyz = 1.768, 1.895, 2.035. The average g-value of 1.902 is typical for nitrogen ligand-containing clusters. EPR spin quantification and the iron content indicate the presence of one [2Fe-2S] cluster. The purified protein displaus ubiquinol cytochrome c reductase activity. The pH optimum of this reaction is temperature dependent and was determined to be pH 7 at 56°C. The results presented in this study clearly prove that the Sulfolobus Rieske protein belongs to the family of the true Rieske iron-sulfur proteins.
| Original language | English |
|---|---|
| Journal | FEBS Letters |
| Volume | 359 |
| Issue number | 2-3 |
| Pages (from-to) | 239-243 |
| Number of pages | 5 |
| ISSN | 0014-5793 |
| DOIs | |
| Publication status | Published - 13.02.1995 |
Funding
Acknowledgements: The authors wish to thank E. Bill for his kind help with the EPR spectroscopy in Lfibeck, R. Schmid for the N-terminal sequence analysis, and Prof. M. Brunori for providing cytochrome c55~ from Pseudomonas aeruginosa. This work was supported by a grant from the European community (EEC project BIO2-CT93-0274), JNICT, Portugal (Grant STRDAdC/BIOI416/92 to M.T.) and grants from the Deutsche Forschungsgemeinschaft (DFG) to S.A. and G.S.
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)
