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ferredoxin
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ferredoxin

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Also known as ferredoxins

Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. They contain iron and sulfur atoms organized as iron–sulfur clusters. These biomolecules accept or discharge electrons, with the effect of a change in the oxidation state of the iron atoms between +2 and +3, letting them act as electron transfer agents in biological redox reactions.

Key facts

Protein family.Symbol
Fer4
Protein family.Name
3Fe-4S binding domain
Protein family.image
Fe3S4.svg
Protein family.caption
Structural representation of an Fe3S4 ferredoxin.
Protein family.Pfam
PF00111
Protein family.Pfam_clan
CL0486
Protein family.InterPro
IPR001450
Protein family.Prosite
PDOC00176
Protein family.SCOP
5fd1
Protein family.OPM protein
1kqf
Protein.Name
ferredoxin 1
Protein.caption
Crystal structure of human ferredoxin-1 (FDX1).
Protein.image
3P1M.pdb1.png
Protein.HGNCid
3638
Protein.Symbol
FDX1
Protein.AltSymbols
FDX
Protein.EntrezGene
2230
Protein.OMIM
103260

via Wikipedia infobox

Research

9,515 papers

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Wikidata facts

Image
3P1M.pdb1.png
Show 1 more fact
Commons category
Ferredoxin
Sources (3)

via Wikidata · CC0

~12 min read

Article

17 sections
Contents
  • Bioenergetics of ferredoxins
  • Reduction of ferredoxin
  • Direct reduction
  • Membrane potential coupled reduction
  • Electron bifurcation
  • Direct reduction of high potential ferredoxins
  • Fe<sub>2</sub>S<sub>2</sub> ferredoxins
  • Plant-type ferredoxins
  • Thioredoxin-like ferredoxins
  • Adrenodoxin-type ferredoxins
  • Fe<sub>4</sub>S<sub>4</sub> and Fe<sub>3</sub>S<sub>4</sub> ferredoxins
  • Bacterial-type ferredoxins
  • High-potential iron–sulfur proteins
  • Human proteins from ferredoxin family
  • References
  • Further reading
  • External links

Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. They contain iron and sulfur atoms organized as iron–sulfur clusters. These biomolecules accept or discharge electrons, with the effect of a change in the oxidation state of the iron atoms between +2 and +3, letting them act as electron transfer agents in biological redox 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.

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