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Purification and characterization of the Rieske iron‐sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius
Author(s) -
Schmidt C.L.,
Anemüller S.,
Teixeira M.,
Schäfer G.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00052-w
Subject(s) - sulfolobus acidocaldarius , sulfolobus , sulfur , archaea , biology , biochemistry , chemistry , organic chemistry , gene
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 g xyz = 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.