Loading
PDBj
メニューPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9FBK

Diheme cytochrome c Kustd1711 from Kuenenia stuttgartiensis, without glycerol cryoprotectant

9FBK の概要
エントリーDOI10.2210/pdb9fbk/pdb
関連するPDBエントリー7zs0 7zs1 7zs2
分子名称Hypothetical (Diheme) protein, CALCIUM ION, HEME C, ... (4 entities in total)
機能のキーワードheme c, anaerobic ammonium oxidation, electron transport
由来する生物種Candidatus Kuenenia
タンパク質・核酸の鎖数1
化学式量合計35732.56
構造登録者
Hauser, D.,Barends, T.R.M. (登録日: 2024-05-14, 公開日: 2024-12-25, 最終更新日: 2025-02-05)
主引用文献Akram, M.,Hauser, D.,Dietl, A.,Steigleder, M.,Ullmann, G.M.,Barends, T.R.M.
Redox potential tuning by calcium ions in a novel c-type cytochrome from an anammox organism.
J.Biol.Chem., 301:108082-108082, 2024
Cited by
PubMed Abstract: The electrochemical potentials of redox-active proteins need to be tuned accurately to the correct values for proper biological function. Here, we describe a diheme cytochrome c with high heme redox potentials of about +350 mV, despite having a large overall negative charge, which typically reduces redox potentials. High-resolution crystal structures, spectroelectrochemical measurements, and high-end computational methods show how this is achieved: each heme iron has a calcium cation positioned next to it at a distance of only 6.9 Å, raising their redox potentials by several hundred millivolts through electrostatic interaction. We suggest that this has evolved to provide the protein with a high redox potential despite its large negative surface charge, which it likely requires for interactions with redox partners.
PubMed: 39675707
DOI: 10.1016/j.jbc.2024.108082
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 9fbk
検証レポート(詳細版)ダウンロードをダウンロード

248942

件を2026-02-11に公開中

PDB statisticsPDBj update infoContact PDBjnumon