9txo | pdb_00009txo
Spinach Ferredoxin I, Re-Oxidised
Structural highlights
FunctionFER1_SPIOL Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Publication Abstract from PubMedIron-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. Crystallise, poise, capture: a multimodal platform for correlated structural and spectroscopic characterisation of redox enzymes.,Laxmi S, Jaho S, Myers WK, Vincent KA, Carr SB J Biol Inorg Chem. 2026 May 5. doi: 10.1007/s00775-026-02148-x. PMID:42082801[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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