9TXE
Spinach Ferredoxin I, Oxidised
9TXE の概要
| エントリーDOI | 10.2210/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 | |
| 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: 42082801DOI: 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) |
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