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9TXE

Spinach Ferredoxin I, Oxidised

9TXE の概要
エントリーDOI10.2210/pdb9txe/pdb
関連するPDBエントリー29KI 9TXO 9TXQ
分子名称Ferredoxin-1, chloroplastic, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
機能のキーワードredox, metalloprotein, iron-sulfur cluster, electron transport
由来する生物種Spinacia oleracea (spinach)
タンパク質・核酸の鎖数1
化学式量合計11449.08
構造登録者
Laxmi, S.,Carr, S.B.,Vincent, K.A. (登録日: 2026-01-15, 公開日: 2026-05-13)
主引用文献Laxmi, S.,Jaho, S.,Myers, W.K.,Vincent, K.A.,Carr, S.B.
Crystallise, poise, capture: a multimodal platform for correlated structural and spectroscopic characterisation of redox enzymes.
J.Biol.Inorg.Chem., 2026
Cited by
PubMed Abstract: Iron-sulfur (Fe-S) clusters are ubiquitous as redox-active protein cofactors, but it is often difficult to collect protein structures in which redox centres are in uniform and well-defined oxidation states. Using spinach ferredoxin I (Fdx) as a model redox protein, we demonstrate an integrated methodological pathway for electrochemical modulation of redox state in protein crystals coupled with in crystallo EPR and online-UV-visible spectroscopy to verify oxidation state. We show that Fdx crystals can be electrochemically reduced, reversibly, without compromising lattice integrity or X-ray diffraction quality. We show that redox levels can be precisely ascertained in crystallo via EPR and UV-visible spectroscopy, enabling a direct correlation between protein structure and electronic state of the metal cluster. In this way, we generate and compare 'oxidised', 'reduced' and 're-oxidised' structures of Fdx. Overall, our approach demonstrates a pipeline which will be applicable to structure-function studies of a wide range of electron-transfer proteins and redox enzymes.
PubMed: 42082801
DOI: 10.1007/s00775-026-02148-x
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (0.95 Å)
構造検証レポート
Validation report summary of 9txe
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-06-17に公開中

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