FDX1

Ferredoxin 1, also known as FDX1, is a human gene.cite web | title = Entrez Gene: FDX1 ferredoxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2230| accessdate = ]

PBB_Summary
section_title =
summary_text = The product of this gene is a small iron-sulfur protein that transfers electrons from NADPH through ferredoxin reductase to a terminal cytochrome P450. This particular oxidation/reduction system is found in steroidogenic tissues, and is involved with the synthesis of bile acid and vitamin D. In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21. This gene product has been identified in a number of different tissues but all forms have been shown to be identical and are not tissue specific.cite web | title = Entrez Gene: FDX1 ferredoxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2230| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Grinberg AV, Hannemann F, Schiffler B, "et al." |title=Adrenodoxin: structure, stability, and electron transfer properties. |journal=Proteins |volume=40 |issue= 4 |pages= 590–612 |year= 2000 |pmid= 10899784 |doi=
*cite journal | author=Wada A, Waterman MR |title=Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. |journal=J. Biol. Chem. |volume=267 |issue= 32 |pages= 22877–82 |year= 1992 |pmid= 1429635 |doi=
*cite journal | author=Sparkes RS, Klisak I, Miller WL |title=Regional mapping of genes encoding human steroidogenic enzymes: P450scc to 15q23-q24, adrenodoxin to 11q22; adrenodoxin reductase to 17q24-q25; and P450c17 to 10q24-q25. |journal=DNA Cell Biol. |volume=10 |issue= 5 |pages= 359–65 |year= 1991 |pmid= 1863359 |doi=
*cite journal | author=Skjeldal L, Markley JL, Coghlan VM, Vickery LE |title=1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins. |journal=Biochemistry |volume=30 |issue= 37 |pages= 9078–83 |year= 1991 |pmid= 1909889 |doi=
*cite journal | author=Coghlan VM, Vickery LE |title=Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc. |journal=J. Biol. Chem. |volume=266 |issue= 28 |pages= 18606–12 |year= 1991 |pmid= 1917982 |doi=
*cite journal | author=Chang CY, Wu DA, Mohandas TK, Chung BC |title=Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family. |journal=DNA Cell Biol. |volume=9 |issue= 3 |pages= 205–12 |year= 1990 |pmid= 2340092 |doi=
*cite journal | author=Mittal S, Zhu YZ, Vickery LE |title=Molecular cloning and sequence analysis of human placental ferredoxin. |journal=Arch. Biochem. Biophys. |volume=264 |issue= 2 |pages= 383–91 |year= 1988 |pmid= 2969697 |doi=
*cite journal | author=Chang CY, Wu DA, Lai CC, "et al." |title=Cloning and structure of the human adrenodoxin gene. |journal=DNA |volume=7 |issue= 9 |pages= 609–15 |year= 1989 |pmid= 3229285 |doi=
*cite journal | author=Voutilainen R, Picado-Leonard J, DiBlasio AM, Miller WL |title=Hormonal and developmental regulation of adrenodoxin messenger ribonucleic acid in steroidogenic tissues. |journal=J. Clin. Endocrinol. Metab. |volume=66 |issue= 2 |pages= 383–8 |year= 1988 |pmid= 3339111 |doi=
*cite journal | author=Picado-Leonard J, Voutilainen R, Kao LC, "et al." |title=Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. |journal=J. Biol. Chem. |volume=263 |issue= 7 |pages= 3240–4 |year= 1988 |pmid= 3343244 |doi=
*cite journal | author=Martsev SP, Chashchin VL, Akhrem AA |title= [Reconstruction and study of a multi-enzyme system by 11 beta-hydroxylase steroids] |journal=Biokhimiia |volume=50 |issue= 2 |pages= 243–57 |year= 1985 |pmid= 3872685 |doi=
*cite journal | author=Geren LM, Millett F |title=Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c. |journal=J. Biol. Chem. |volume=256 |issue= 20 |pages= 10485–9 |year= 1981 |pmid= 6270113 |doi=
*cite journal | author=Pikuleva IA, Cao C, Waterman MR |title=An additional electrostatic interaction between adrenodoxin and P450c27 (CYP27A1) results in tighter binding than between adrenodoxin and p450scc (CYP11A1). |journal=J. Biol. Chem. |volume=274 |issue= 4 |pages= 2045–52 |year= 1999 |pmid= 9890963 |doi=
*cite journal | author=Kostic M, Pochapsky SS, Obenauer J, "et al." |title=Comparison of functional domains in vertebrate-type ferredoxins. |journal=Biochemistry |volume=41 |issue= 19 |pages= 5978–89 |year= 2002 |pmid= 11993992 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Johnson D, Norman S, Tuckey RC, Martin LL |title=Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode. |journal=Bioelectrochemistry (Amsterdam, Netherlands) |volume=59 |issue= 1-2 |pages= 41–7 |year= 2004 |pmid= 12699818 |doi=
*cite journal | author=Araya Z, Hosseinpour F, Bodin K, Wikvall K |title=Metabolism of 25-hydroxyvitamin D3 by microsomal and mitochondrial vitamin D3 25-hydroxylases (CYP2D25 and CYP27A1): a novel reaction by CYP27A1. |journal=Biochim. Biophys. Acta |volume=1632 |issue= 1-3 |pages= 40–7 |year= 2003 |pmid= 12782149 |doi=
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Derouet-Hümbert E, Roemer K, Bureik M |title=Adrenodoxin (Adx) and CYP11A1 (P450scc) induce apoptosis by the generation of reactive oxygen species in mitochondria. |journal=Biol. Chem. |volume=386 |issue= 5 |pages= 453–61 |year= 2005 |pmid= 15927889 |doi= 10.1515/BC.2005.054

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