| Description | Ferredoxins are iron-sulphur proteins that mediate electron transfer in a range of metabolic reactions [ , ]; they fall into several subgroups according to the nature of their iron-sulphur cluster(s). One group, originally found in chloroplast membranes, has been termed 'chloroplast-type' or 'plant-type', and includes ferredoxins from plants, algae, archaea, rhodobacter and a toluene degrading pseudomonas. Here, the active centre is a 2Fe-2S cluster, where the irons are tetrahedrally coordinated by both inorganic sulphurs and sulphurs provided by 4 conserved Cys residues []. In chloroplasts, 2Fe-2S ferredoxins function as electron carriers in the photosynthetic electron transport chain and as electron donors to various cellular proteins. In hydroxylating bacterial dioxygenase systems, they serve as intermediate electron-transfer carriers between reductase flavoproteins and oxygenase [].Several oxidoreductases contain redox domains similar to 2Fe-2S ferredoxins, including ferredoxin/ferredoxin reductase components of several bacterial aromatic di- and monooxygenases, phenol hydroxylase, methane monooxygenase, vanillate demethylase oxidoreductase, phthalate dioxygenase reductase, bacterial fumarate reductase iron-sulphur protein, eukaryotic succinate dehydrogenase and xanthine dehydrogenase. 3D structures are known for a number of 2Fe-2S ferredoxins [ ] and for the ferredoxin reductase/ferredoxin fusion protein phthalate dioxygenase reductase []. The fold belongs to the α + β class, with 3 helices and 4 strands forming a barrel-like structure, and an extruded loop containing 3 of the 4 cysteinyl residues of the iron-sulphur cluster.In the 2Fe-2S ferredoxins, four cysteine residues bind the iron-sulphur cluster. Three of these cysteines are clustered together in the same region of the protein. This sequence cover the three cysteine residues involved in iron-sulphur binding. | Name | 2Fe-2S ferredoxin, iron-sulphur binding site |
| Short Name | 2Fe2S_fd_BS | Type | Binding_site |
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