1996年4月
Isolation, characterisation and crystallisation of a water-soluble fragment of the Rieske iron-sulfur protein of bovine heart mitochondrial bc(1) complex
EUROPEAN JOURNAL OF BIOCHEMISTRY
- ,
- ,
- ,
- ,
- ,
- 巻
- 237
- 号
- 1
- 開始ページ
- 71
- 終了ページ
- 75
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1111/j.1432-1033.1996.0071n.x
- 出版者・発行元
- SPRINGER VERLAG
A water-soluble fragment of the be, complex from bovine heart mitochondria was isolated containing the intact Rieske [2Fe-2S] cluster. The fragment consists of the last 129 amino acid residues of the Rieske iron-sulfur protein and has a molecular mass of 14592 Da including two iron atoms. The absorption, visible CD, and EPR spectra of the fragment are indistinguishable from those of the membrane-bound iron-sulfur protein. The redox potential as determined by EPR-monitored redox titration was +306 mV. The far-ultraviolet CD spectrum is indicative of a protein with little regular secondary structure, while significant a-helix content was detected in the membrane anchor of the complete iron-sulfur protein. The fragment could be crystallized using poly(ethylene glycol) 6000 as precipitant. Needle-shaped single crystals have been grown by the hanging-drop vapor diffusion technique. These crystals belong to the space group P2(1) and diffract well beyond 0.2 nm resolution. Phase determination using the multiple-wavelength anomalous-scattering technique is underway.
- リンク情報
- ID情報
-
- DOI : 10.1111/j.1432-1033.1996.0071n.x
- ISSN : 0014-2956
- Web of Science ID : WOS:A1996UD77400008