1RIE

STRUCTURE OF A WATER SOLUBLE FRAGMENT OF THE RIESKE IRON-SULFUR PROTEIN OF THE BOVINE HEART MITOCHONDRIAL CYTOCHROME BC1-COMPLEX

1RIE の概要

• エントリーDOI: 10.2210/pdb1rie/pdb
• 分子名称: RIESKE IRON-SULFUR PROTEIN, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• 機能のキーワード: oxidoreductase, cytochrome bc1 complex, histidine ligands, rieske iron-sulfur cluster, electron transport
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Mitochondrion inner membrane: P13272
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14616.48

構造登録者

Iwata, S.,Saynovits, M.,Link, T.A.,Michel, H. (登録日: 1996-02-23, 公開日: 1996-12-07, 最終更新日: 2024-10-23)

主引用文献

Iwata, S.,Saynovits, M.,Link, T.A.,Michel, H.
Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 A resolution.
Structure, 4:567-579, 1996

PubMed Abstract: The 'Rieske' iron-sulfur protein is the primary electron acceptor during hydroquinone oxidation in cytochrome bc complexes. The spectroscopic and electrochemical properties of the 'Rieske' [2Fe-2S] cluster differ significantly from those of other iron-sulfur clusters. A 129-residue water soluble fragment containing the intact [2Fe-2S] cluster was isolated following proteolytic digestion of the bc1 complex and used for structural studies.

PubMed: 8736555
DOI: 10.1016/S0969-2126(96)00062-7

実験手法

X-RAY DIFFRACTION (1.5 Å)