9GYU
Ferredoxin CNF-labelled reduced state
Summary for 9GYU
| Entry DOI | 10.2210/pdb9gyu/pdb |
| Descriptor | Ferredoxin-1, chloroplastic, FE2/S2 (INORGANIC) CLUSTER (3 entities in total) |
| Functional Keywords | metalloprotein iron-sulfur cluster electron transfer, oxidoreductase |
| Biological source | Spinacia oleracea (spinach) |
| Total number of polymer chains | 1 |
| Total formula weight | 11458.09 |
| Authors | |
| Primary citation | Duan, Z.,Wei, J.,Carr, S.B.,Ramirez, M.,Evans, R.M.,Ash, P.A.,Rodriguez-Macia, P.,Sachdeva, A.,Vincent, K.A. Cyanophenylalanine as an Infrared Probe for Iron-Sulfur Cluster Redox State in Multi-Centre Metalloenzymes. Chembiochem, :e202500251-e202500251, 2025 Cited by PubMed Abstract: The noncanonical amino acid, para-cyanophenylalanine (CNF), when incorporated into metalloproteins, functions as an infrared spectroscopic probe for the redox state of iron-sulfur clusters, offering a strategy for determining electron occupancy in the electron transport chains of complex metalloenzymes. A redshift of ≈1-2 cm in the nitrile (NC) stretching frequency is observed, following reduction of spinach ferredoxin modified to contain CNF close to its [2Fe-2S] center, and this shift is reversed on re-oxidation. We extend this to CNF positioned near to the proximal [4Fe-4S] cluster of the [FeFe] hydrogenase from Desulfovibrio desulfuricans. In combination with a distal [4Fe-4S] cluster and the [4Fe-4S] cluster of the active site 'H-cluster' ([4Fe-4S]), the proximal cluster forms an electron relay connecting the active site to the surface of the protein. Again, a reversible shift in wavenumber for CNF is observed, following cluster reduction in either apo-protein (containing the iron-sulfur clusters but lacking the active site) or holo-protein with intact active site, demonstrating the general applicability of this approach to studying complex metalloenzymes. PubMed: 40347495DOI: 10.1002/cbic.202500251 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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