Adrenal ferredoxin
{{Short description|Mammalian protein found in Homo sapiens}}
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Adrenal ferredoxin (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that in humans is encoded by the FDX1 gene.{{cite journal | vauthors = 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 |date=Sep 1988 | pmid = 2969697 | doi =10.1016/0003-9861(88)90303-7 }}{{cite web | title = Entrez Gene: FDX1 ferredoxin 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2230}} 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.{{cite journal | vauthors = Hanukoglu I, Jefcoate CR | title = Mitochondrial cytochrome P-450scc. Mechanism of electron transport by adrenodoxin | journal = The Journal of Biological Chemistry | volume = 255 | issue = 7 | pages = 3057–61 | date = Apr 1980 | doi = 10.1016/S0021-9258(19)85851-9 | pmid = 6766943 | url = http://www.jbc.org/content/255/7/3057.full.pdf | doi-access = free }} The first enzyme in this system is adrenodoxin reductase that carries an FAD. FAD can be reduced by two electrons donated from coenzyme NADPH.{{cite journal | vauthors = Hanukoglu I | title = Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme | journal = Journal of Molecular Evolution | volume = 85 | issue= 5 | pages= 205–218 | year= 2017 | pmid= 29177972 | doi= 10.1007/s00239-017-9821-9 | bibcode = 2017JMolE..85..205H | s2cid = 7120148 }} These two electrons are transferred one a time to adrenodoxin. Adrenodoxin in return reduces mitochondrial cytochrome P450. 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.
References
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Further reading
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- {{cite journal | vauthors=Grinberg AV, Hannemann F, Schiffler B |title=Adrenodoxin: structure, stability, and electron transfer properties |journal=Proteins |volume=40 |issue= 4 |pages= 590–612 |year= 2000 |pmid= 10899784 |doi=10.1002/1097-0134(20000901)40:4<590::AID-PROT50>3.0.CO;2-P |s2cid=113757 |display-authors=etal}}
- {{cite journal | vauthors=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 |doi=10.1016/S0021-9258(18)50028-4 |pmid= 1429635 |doi-access=free }}
- {{cite journal | vauthors=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=10.1089/dna.1991.10.359 }}
- {{cite journal | vauthors=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=10.1021/bi00101a024 }}
- {{cite journal | vauthors=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 |doi=10.1016/S0021-9258(18)55106-1 |pmid= 1917982 |doi-access=free }}
- {{cite journal | vauthors=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=10.1089/dna.1990.9.205 }}
- {{cite journal | vauthors=Chang CY, Wu DA, Lai CC |title=Cloning and structure of the human adrenodoxin gene |journal=DNA |volume=7 |issue= 9 |pages= 609–15 |year= 1989 |pmid= 3229285 |doi=10.1089/dna.1988.7.609 |display-authors=etal}}
- {{cite journal | vauthors=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=10.1210/jcem-66-2-383 }}
- {{cite journal | vauthors=Picado-Leonard J, Voutilainen R, Kao LC |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 |doi=10.1016/S0021-9258(18)69061-1 |pmid= 3343244 |display-authors=etal|doi-access=free }}
- {{cite journal | vauthors=Martsev SP, Chashchin VL, Akhrem AA | author3-link = :be:Афанасій Андрэевіч Ахрэм |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 }}
- {{cite journal | vauthors=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 |doi=10.1016/S0021-9258(19)68647-3 |pmid= 6270113 |doi-access=free }}
- {{cite journal | vauthors=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=10.1074/jbc.274.4.2045 |doi-access= free}}
- {{cite journal | vauthors=Kostic M, Pochapsky SS, Obenauer J |title=Comparison of functional domains in vertebrate-type ferredoxins |journal=Biochemistry |volume=41 |issue= 19 |pages= 5978–89 |year= 2002 |pmid= 11993992 |doi=10.1021/bi0200256 |display-authors=etal}}
- {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 | pmc=139241 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
- {{cite journal | vauthors=Johnson D, Norman S, Tuckey RC, Martin LL |title=Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode |journal= Bioelectrochemistry|volume=59 |issue= 1–2 |pages= 41–7 |year= 2004 |pmid= 12699818 |doi= 10.1016/s1567-5394(02)00188-3|doi-access=free }}
- {{cite journal | vauthors=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= 10.1016/S1388-1981(03)00062-3}}
- {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |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 | pmc=528928 |display-authors=etal}}
- {{cite journal | vauthors=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 |s2cid=37533711 }}
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External links
- {{UCSC gene info|FDX1}}
{{PDB Gallery|geneid=2230}}
{{gene-11-stub}}