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• W4247133074 abstract "Abstract The 2Fe ferredoxins (Fds) are simple iron–sulfur proteins, containing one 2Fe–2S cluster, that are involved mainly as electron carriers of low oxidation–reduction potential in fundamental metabolic processes. They can be subdivided into three families: class I, plant‐type; class II, adrenodoxin‐type; and class III, Clostridium ‐type; according to the spacing in the sequence of the cysteinyl residues that bind the iron atoms of the cluster. All the Fds are monomers of 11–14 kDa, except for class III Fds that are dimer, with one cluster per subunit. The cluster of 2Fe Fds contains two atoms of iron, bridged by two acid‐labile inorganic sulfide atoms, and coordinated to four cysteinyl sulfurs of the polypeptide chain. Fds absorb light in the 300–500 nm visible region, mainly due to sulfur‐Fe 3+ charge‐transfer transitions. The cluster in the oxidized protein contains two antiferromagnetically coupled, high‐spin (S = 5/2) ferric irons and is, therefore, electron paramagnetic resonance (EPR) silent. Upon one‐electron reduction, Fds become paramagnetic. The three‐dimensional (3D) structure of several 2Fe Fds have been obtained either by X‐ray crystallography or by n uclear magnetic resonance (NMR) spectroscopy. The solution structures are very similar to the 3D crystal structures. The protein structure motif characteristic of Fds has been named β‐grasp – a five‐stranded antiparallel β‐sheet with an α‐helix lying on top of the sheet. This central core (β1–β5 and α1) is surrounded by two short β‐strands, an α‐helix (α2), and a short C‐terminal helical turn (α3). Class II Fds have an additional interaction domain. Comparison of the structures of the different proteins reveals conformational differences especially between class I and II ferredoxins. The binuclear iron cluster lies in a solvent‐exposed pocket generated by the loop connecting helix α1 and strand β3 and comprising three of the cysteinyl ligands. This loop is anchored through several hydrogen bonds to different parts of the protein molecule. An extensive survey of the literature on the interactions of several 2Fe Fds with their respective partners is presented." @default.
• W4247133074 created "2022-05-12" @default.
• W4247133074 creator A5021999579 @default.
• W4247133074 creator A5043213044 @default.
• W4247133074 creator A5070368745 @default.
• W4247133074 date "2004-03-05" @default.
• W4247133074 modified "2023-09-29" @default.
• W4247133074 title "The [2Fe-2S] Ferredoxins" @default.
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