Purification and characterization of the Rieske iron‐sulfur protein from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius

FEBS Letters

Anemüller, S.²  Schäfer, G.²  Schmidt, C.L.²  Teixeira, M.¹ 

[1] Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apt. 127, Rua da Quinta Grande 6, 2780 Oeiras, Portugal;Institut für Biochemie, Medizinische Universität zu Lübeck, Ratzeburger Alle 160, 23538 Lübeck, Germany

关键词: Rieske;    Archaea;    Iron-sulfur protein;    Ubiquinol cytochrome c reductase;    EPR;   

DOI  :  10.1016/0014-5793(94)00052-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown