Adrenal ferredoxin (also adrenodoxin (ADX), adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin-1 (FDX1)) is a protein that in humans is encoded by the FDX1gene.[5][6] In addition to the expressed gene at this chromosomal locus (11q22), there are pseudogenes located on chromosomes 20 and 21.
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]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000137714 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000032051 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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.
^ abHanukoglu 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.
^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 readingedit
Grinberg AV, Hannemann F, Schiffler B, et al. (2000). "Adrenodoxin: structure, stability, and electron transfer properties". Proteins. 40 (4): 590–612. doi:10.1002/1097-0134(20000901)40:4<590::AID-PROT50>3.0.CO;2-P. PMID 10899784. S2CID 113757.
Wada A, Waterman MR (1992). "Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding". J. Biol. Chem. 267 (32): 22877–82. doi:10.1016/S0021-9258(18)50028-4. PMID 1429635.
Sparkes RS, Klisak I, Miller WL (1991). "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". DNA Cell Biol. 10 (5): 359–65. doi:10.1089/dna.1991.10.359. PMID 1863359.
Skjeldal L, Markley JL, Coghlan VM, Vickery LE (1991). "1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins". Biochemistry. 30 (37): 9078–83. doi:10.1021/bi00101a024. PMID 1909889.
Coghlan VM, Vickery LE (1991). "Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc". J. Biol. Chem. 266 (28): 18606–12. doi:10.1016/S0021-9258(18)55106-1. PMID 1917982.
Chang CY, Wu DA, Mohandas TK, Chung BC (1990). "Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family". DNA Cell Biol. 9 (3): 205–12. doi:10.1089/dna.1990.9.205. PMID 2340092.
Chang CY, Wu DA, Lai CC, et al. (1989). "Cloning and structure of the human adrenodoxin gene". DNA. 7 (9): 609–15. doi:10.1089/dna.1988.7.609. PMID 3229285.
Voutilainen R, Picado-Leonard J, DiBlasio AM, Miller WL (1988). "Hormonal and developmental regulation of adrenodoxin messenger ribonucleic acid in steroidogenic tissues". J. Clin. Endocrinol. Metab. 66 (2): 383–8. doi:10.1210/jcem-66-2-383. PMID 3339111.
Picado-Leonard J, Voutilainen R, Kao LC, et al. (1988). "Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells". J. Biol. Chem. 263 (7): 3240–4. doi:10.1016/S0021-9258(18)69061-1. PMID 3343244.
Martsev SP, Chashchin VL, Akhrem AA [in Belarusian] (1985). "[Reconstruction and study of a multi-enzyme system by 11 beta-hydroxylase steroids]". Biokhimiia. 50 (2): 243–57. PMID 3872685.
Geren LM, Millett F (1981). "Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c". J. Biol. Chem. 256 (20): 10485–9. doi:10.1016/S0021-9258(19)68647-3. PMID 6270113.
Pikuleva IA, Cao C, Waterman MR (1999). "An additional electrostatic interaction between adrenodoxin and P450c27 (CYP27A1) results in tighter binding than between adrenodoxin and p450scc (CYP11A1)". J. Biol. Chem. 274 (4): 2045–52. doi:10.1074/jbc.274.4.2045. PMID 9890963.
Kostic M, Pochapsky SS, Obenauer J, et al. (2002). "Comparison of functional domains in vertebrate-type ferredoxins". Biochemistry. 41 (19): 5978–89. doi:10.1021/bi0200256. PMID 11993992.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Johnson D, Norman S, Tuckey RC, Martin LL (2004). "Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode". Bioelectrochemistry. 59 (1–2): 41–7. doi:10.1016/s1567-5394(02)00188-3. PMID 12699818.
Araya Z, Hosseinpour F, Bodin K, Wikvall K (2003). "Metabolism of 25-hydroxyvitamin D3 by microsomal and mitochondrial vitamin D3 25-hydroxylases (CYP2D25 and CYP27A1): a novel reaction by CYP27A1". Biochim. Biophys. Acta. 1632 (1–3): 40–7. doi:10.1016/S1388-1981(03)00062-3. PMID 12782149.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC528928. PMID 15489334.
Derouet-Hümbert E, Roemer K, Bureik M (2005). "Adrenodoxin (Adx) and CYP11A1 (P450scc) induce apoptosis by the generation of reactive oxygen species in mitochondria". Biol. Chem. 386 (5): 453–61. doi:10.1515/BC.2005.054. PMID 15927889. S2CID 37533711.
External linksedit
Human FDX1 genome location and FDX1 gene details page in the UCSC Genome Browser.
This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by expanding it.
adrenal, ferredoxin, also, adrenodoxin, adrenodoxin, mitochondrial, hepatoredoxin, ferredoxin, fdx1, protein, that, humans, encoded, fdx1, gene, addition, expressed, gene, this, chromosomal, locus, 11q22, there, pseudogenes, located, chromosomes, fdx1available. Adrenal ferredoxin also adrenodoxin ADX adrenodoxin mitochondrial hepatoredoxin ferredoxin 1 FDX1 is a protein that in humans is encoded by the FDX1 gene 5 6 In addition to the expressed gene at this chromosomal locus 11q22 there are pseudogenes located on chromosomes 20 and 21 FDX1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes3N9Y 3N9Z 3NA0 3NA1 3P1MIdentifiersAliasesFDX1 ADX FDX LOH11CR1D ferredoxin 1External IDsOMIM 103260 MGI 103224 HomoloGene 31216 GeneCards FDX1Gene location Human Chr Chromosome 11 human 1 Band11q22 3Start110 429 948 bp 1 End110 464 884 bp 1 Gene location Mouse Chr Chromosome 9 mouse 2 Band9 9 A5 3Start51 854 606 bp 2 End51 874 856 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inleft adrenal glandseminal vesiculakidney tubulejejunal mucosaamniotic fluidright ventricleparotid glandplacentathoracic diaphragmpalpebral conjunctivaTop expressed inadrenal glandleft lobe of liverinterventricular septumPaneth cellbrown adipose tissuevastus lateralis musclesternocleidomastoid muscleproximal tubuledigastric muscleaortic valveMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functioniron ion binding electron transfer activity iron sulfur cluster binding metal ion binding 2 iron 2 sulfur cluster bindingCellular componentmitochondrion mitochondrial matrixBiological processC21 steroid hormone biosynthetic process sterol metabolic process cholesterol metabolic process small molecule metabolic process hormone biosynthetic process lipid metabolism steroid biosynthetic process steroid metabolic process cellular response to cAMP cellular response to forskolin electron transport chainSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez223014148EnsemblENSG00000137714ENSMUSG00000032051UniProtP10109P46656RefSeq mRNA NM 004109NM 001301728NM 007996RefSeq protein NP 004100NP 001288657NP 032022Location UCSC Chr 11 110 43 110 46 MbChr 9 51 85 51 87 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 References 3 Further reading 4 External linksFunction editAdrenodoxin 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 edit a b c GRCh38 Ensembl release 89 ENSG00000137714 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000032051 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 a b Entrez Gene FDX1 ferredoxin 1 a b 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 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 editGrinberg AV Hannemann F Schiffler B et al 2000 Adrenodoxin structure stability and electron transfer properties Proteins 40 4 590 612 doi 10 1002 1097 0134 20000901 40 4 lt 590 AID PROT50 gt 3 0 CO 2 P PMID 10899784 S2CID 113757 Wada A Waterman MR 1992 Identification by site directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding J Biol Chem 267 32 22877 82 doi 10 1016 S0021 9258 18 50028 4 PMID 1429635 Sparkes RS Klisak I Miller WL 1991 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 DNA Cell Biol 10 5 359 65 doi 10 1089 dna 1991 10 359 PMID 1863359 Skjeldal L Markley JL Coghlan VM Vickery LE 1991 1H NMR spectra of vertebrate 2Fe 2S ferredoxins Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins Biochemistry 30 37 9078 83 doi 10 1021 bi00101a024 PMID 1909889 Coghlan VM Vickery LE 1991 Site specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc J Biol Chem 266 28 18606 12 doi 10 1016 S0021 9258 18 55106 1 PMID 1917982 Chang CY Wu DA Mohandas TK Chung BC 1990 Structure sequence chromosomal location and evolution of the human ferredoxin gene family DNA Cell Biol 9 3 205 12 doi 10 1089 dna 1990 9 205 PMID 2340092 Chang CY Wu DA Lai CC et al 1989 Cloning and structure of the human adrenodoxin gene DNA 7 9 609 15 doi 10 1089 dna 1988 7 609 PMID 3229285 Voutilainen R Picado Leonard J DiBlasio AM Miller WL 1988 Hormonal and developmental regulation of adrenodoxin messenger ribonucleic acid in steroidogenic tissues J Clin Endocrinol Metab 66 2 383 8 doi 10 1210 jcem 66 2 383 PMID 3339111 Picado Leonard J Voutilainen R Kao LC et al 1988 Human adrenodoxin cloning of three cDNAs and cycloheximide enhancement in JEG 3 cells J Biol Chem 263 7 3240 4 doi 10 1016 S0021 9258 18 69061 1 PMID 3343244 Martsev SP Chashchin VL Akhrem AA in Belarusian 1985 Reconstruction and study of a multi enzyme system by 11 beta hydroxylase steroids Biokhimiia 50 2 243 57 PMID 3872685 Geren LM Millett F 1981 Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c J Biol Chem 256 20 10485 9 doi 10 1016 S0021 9258 19 68647 3 PMID 6270113 Pikuleva IA Cao C Waterman MR 1999 An additional electrostatic interaction between adrenodoxin and P450c27 CYP27A1 results in tighter binding than between adrenodoxin and p450scc CYP11A1 J Biol Chem 274 4 2045 52 doi 10 1074 jbc 274 4 2045 PMID 9890963 Kostic M Pochapsky SS Obenauer J et al 2002 Comparison of functional domains in vertebrate type ferredoxins Biochemistry 41 19 5978 89 doi 10 1021 bi0200256 PMID 11993992 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Johnson D Norman S Tuckey RC Martin LL 2004 Electrochemical behaviour of human adrenodoxin on a pyrolytic graphite electrode Bioelectrochemistry 59 1 2 41 7 doi 10 1016 s1567 5394 02 00188 3 PMID 12699818 Araya Z Hosseinpour F Bodin K Wikvall K 2003 Metabolism of 25 hydroxyvitamin D3 by microsomal and mitochondrial vitamin D3 25 hydroxylases CYP2D25 and CYP27A1 a novel reaction by CYP27A1 Biochim Biophys Acta 1632 1 3 40 7 doi 10 1016 S1388 1981 03 00062 3 PMID 12782149 Gerhard DS Wagner L Feingold EA et al 2004 The status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Derouet Humbert E Roemer K Bureik M 2005 Adrenodoxin Adx and CYP11A1 P450scc induce apoptosis by the generation of reactive oxygen species in mitochondria Biol Chem 386 5 453 61 doi 10 1515 BC 2005 054 PMID 15927889 S2CID 37533711 External links editHuman FDX1 genome location and FDX1 gene details page in the UCSC Genome Browser nbsp This article on a gene on human chromosome 11 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Adrenal ferredoxin amp oldid 1198559682, wikipedia, wiki, book, books, library,
