ferredoxin
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).
Article
17 sectionsContents
- 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.