2N9I

Solution structure of reduced human cytochrome c

2N9I の概要

• エントリーDOI: 10.2210/pdb2n9i/pdb
• 関連するPDBエントリー: 2N9J
• NMR情報: BMRB: 25907
• 分子名称: Cytochrome c, HEME C (2 entities in total)
• 機能のキーワード: cytochrome c, electron transfer, electron transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion intermembrane space: P99999
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12259.09

構造登録者

Imai, M.,Saio, T.,Kumeta, H.,Uchida, T.,Inagaki, F.,Ishimori, K. (登録日: 2015-11-24, 公開日: 2016-02-17, 最終更新日: 2024-11-20)

主引用文献

Imai, M.,Saio, T.,Kumeta, H.,Uchida, T.,Inagaki, F.,Ishimori, K.
Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c
Biochem.Biophys.Res.Commun., 469:978-984, 2016

PubMed Abstract: Redox-dependent changes in the structure and dynamics of human cytochrome c (Cyt c) were investigated by solution NMR. We found significant structural changes in several regions, including residues 23-28 (loop 3), which were further corroborated by chemical shift differences between the reduced and oxidized states of Cyt c. These differences are essential for discriminating redox states in Cyt c by cytochrome c oxidase (CcO) during electron transfer reactions. Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments identified that the region around His33 undergoes conformational exchanges on the μs-ms timescale, indicating significant redox-dependent structural changes. Because His33 is not part of the interaction site for CcO, our data suggest that the dynamic properties of the region, which is far from the interaction site for CcO, contribute to conformational changes during electron transfer to CcO.

PubMed: 26718409
DOI: 10.1016/j.bbrc.2015.12.079

実験手法

SOLUTION NMR