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Ferrodoxin

2Fe-2S iron-sulfur cluster binding domain
Fe2S2.svg
Structural representation of an Fe2S2 ferredoxin.
Identifiers
Symbol Fer2
Pfam PF00111
InterPro IPR001041
PROSITE PDOC00642
SCOP 3fxc
SUPERFAMILY 3fxc
OPM protein 1kf6
ferredoxin 1
3P1M.pdb1.png
Crystal structure of human ferredoxin-1 (FDX1).
Identifiers
Symbol FDX1
Alt. symbols FDX
Entrez 2230
HUGO 3638
OMIM 103260
RefSeq NM_004109
UniProt P10109
Other data
Locus Chr. 11 q22.3
3Fe-4S binding domain
Fe3S4.png
Structural representation of an Fe3S4 ferredoxin.
Identifiers
Symbol Fer4
Pfam PF00037
InterPro IPR001450
PROSITE PDOC00176
SCOP 5fd1
SUPERFAMILY 5fd1
OPM protein 1kqf

Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron-sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.

Another redox protein, isolated from spinach chloroplasts, was termed "chloroplast ferredoxin". The chloroplast ferredoxin is involved in both cyclic and non-cyclic photophosphorylation reactions of photosynthesis. In non-cyclic photophosphorylation, ferredoxin is the last electron acceptor thus reducing the enzyme NADP+ reductase. It accepts electrons produced from sunlight-excited chlorophyll and transfers them to the enzyme ferredoxin: NADP+ oxidoreductase EC 1.18.1.2.

Ferredoxins are small proteins containing iron and sulfur atoms organized as iron-sulfur clusters. These biological "capacitors" can accept or discharge electrons, with the effect of a change in the oxidation state of the iron atoms between +2 and +3. In this way, ferredoxin acts as an electron transfer agent in biological redox reactions.

Other bioinorganic electron transport systems include rubredoxins, , blue copper proteins, and the structurally related Rieske proteins.


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Wikipedia

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