3H1J

Stigmatellin-bound cytochrome bc1 complex from chicken

3H1J の概要

• エントリーDOI: 10.2210/pdb3h1j/pdb
• 関連するPDBエントリー: 1sqx 2bcc 2pp9 3H1H 3H1I 3H1K 3H1L 3cx5
• 分子名称: MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I, MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN, UNKNOWN LIGAND, ... (21 entities in total)
• 機能のキーワード: cytochrome bc1, membrane protein, heme protein, rieske iron sulfur protein, cytochrome b, cytochrome c1, complex iii, mitochondrial processing protein, ubiquinone, oxidoreductase, redox enzym respiratory chain, electron transport, heme, inner membrane iron, membrane, metal-binding, mitochondrion, transmembrane, stigmatellin, iron, mitochondrion inner membrane, respiratory chain, transport, disulfide bond, iron-sulfur, transit peptide
• 由来する生物種: Gallus gallus (chicken); 詳細
• 細胞内の位置: Mitochondrion inner membrane ; Multi-pass membrane protein : P18946; Mitochondrion inner membrane ; Single-pass membrane protein : Q5ZLR5 Q5ZLR5
• タンパク質・核酸の鎖数: 20
• 化学式量合計: 480625.65

構造登録者

Zhang, Z.,Huang, L.,Shulmeister, V.M.,Chi, Y.-I.,Kim, K.K.,Hung, L.-W.,Crofts, A.R.,Berry, E.A.,Kim, S.-H. (登録日: 2009-04-12, 公開日: 2009-04-28, 最終更新日: 2023-09-06)

主引用文献

Zhang, Z.,Huang, L.-S.,Shulmeister, V.M.,Chi, Y.I.,Kim, K.K.,Hung, L.W.,Crofts, A.R.,Berry, E.A.,Kim, S.-H.
Electron Transfer by Domain Movement in Cytochrome Bc1
Nature, 392:677-684, 1998

PubMed Abstract: The cytochrome bc1 is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome bc1 transfers electrons from ubiquinol to cytochrome c and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron-sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe-S protein by ubiquinol. The other site is close enough to cytochrome c1 to allow oxidation of the Fe-S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe-S component in order to shuttle electrons from ubiquinol to cytochrome c1. Such a mechanism has not previously been observed in redox protein complexes.

PubMed: 9565029

実験手法

X-RAY DIFFRACTION (3 Å)