Article · Wikipedia archive · Last revised Jun 7, 2026

Adrenal ferredoxin

Adrenal ferredoxin is a protein that in humans is encoded by the FDX1 gene. In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.

Last revised
Jun 7, 2026
Read time
≈ 5 min
Length
1,048 w
Citations
14
Source
FDX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesFDX1, ADX, FDX, LOH11CR1D, ferredoxin 1
External IDsOMIM: 103260; MGI: 103224; HomoloGene: 31216; GeneCards: FDX1; OMA:FDX1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004109

NM_001301728
NM_007996

RefSeq (protein)

NP_004100

NP_001288657
NP_032022

Location (UCSC)Chr 11: 110.43 – 110.46 MbChr 9: 51.85 – 51.87 Mb
PubMed search34
Wikidata
View/Edit HumanView/Edit Mouse

Adrenal ferredoxin (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that in humans is encoded by the FDX1 gene.56 In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.

Function

Adrenodoxin is a small iron-sulfur protein that can accept and carry a single electron. Adrenodoxin functions as an electron transfer protein in the mitochondrial cytochrome P450 systems.7 The first enzyme in this system is adrenodoxin reductase that carries an FAD. FAD can be reduced by two electrons donated from coenzyme NADPH.8 These two electrons are transferred one a time to adrenodoxin. Adrenodoxin in return reduces mitochondrial cytochrome P450.7 This particular oxidation/reduction system is involved in the synthesis of steroid hormones in steroidogenic tissues. In addition, similar systems also function in vitamin D and bile acid synthesis in the kidney and liver respectively. Adrenodoxin has been identified in a number of different tissues but all forms have been shown to be identical and are not tissue specific.6

References

References

  1. GRCh38: Ensembl release 89: ENSG00000137714Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000032051Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Mittal S, Zhu YZ, Vickery LE (Sep 1988). "Molecular cloning and sequence analysis of human placental ferredoxin". Arch Biochem Biophys. 264 (2): 383–91. doi:10.1016/0003-9861(88)90303-7. PMID 2969697.
  6. "Entrez Gene: FDX1 ferredoxin 1".
  7. Hanukoglu I, Jefcoate CR (Apr 1980). "Mitochondrial cytochrome P-450scc. Mechanism of electron transport by adrenodoxin" (PDF). The Journal of Biological Chemistry. 255 (7): 3057–61. doi:10.1016/S0021-9258(19)85851-9. PMID 6766943.
  8. Hanukoglu I (2017). "Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme". Journal of Molecular Evolution. 85 (5): 205–218. Bibcode:2017JMolE..85..205H. doi:10.1007/s00239-017-9821-9. PMID 29177972. S2CID 7120148.
Further reading

Further reading

External links