The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

FDXR  -  ferredoxin reductase

Homo sapiens

Synonyms: ADXR, AR, Adrenodoxin reductase, Ferredoxin reductase, Ferredoxin--NADP(+) reductase, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of FDXR


High impact information on FDXR


Chemical compound and disease context of FDXR


Biological context of FDXR

  • We found that FDXR can be induced by DNA damage in cells in a p53-dependent manner and by a mutated form of p53 that is competent in inducing apoptosis [13].
  • In addition, we identified a p53 response element located within the FDXR promoter that is responsive to wild-type p53, p63alpha, p63gamma, p73alpha, and p73beta [13].
  • In contrast, substitutions at positions 76 and 79 (D76N and D79A) caused dramatic decreases in activity and in the affinity of ferredoxin for both Fd-reductase and P450scc; this suggests that the binding sites on ferredoxin for its redox partners overlap [1].
  • The AR gene is X-linked and the protein is coded for by eight exons, giving rise to a C-terminal LBD (ligand-binding domain; exons 4-8), linked by a hinge region (exon 4) to a Zn-finger DBD (DNA-binding domain; exons 2 and 3) and a large structurally distinct NTD (N-terminal domain; exon 1) [2].
  • Adrenodoxin reductase (ferrodoxin:NADP+ oxidoreductase, EC is a flavoprotein mediating electron transport to all mitochondrial forms of cytochrome P450 [14].

Anatomical context of FDXR


Associations of FDXR with chemical compounds

  • Increasing either the cholesterol or P450scc concentration increased the amount of AR required for P450scc to work at half its maximum velocity [15].
  • In order to better understand which components of the cholesterol side-chain cleavage system are important in the regulation of placental progesterone synthesis, we have examined their effects on P450scc activity with both saturating and limiting concentrations of AR [15].
  • The AR (androgen receptor) is a ligand-activated transcription factor that mediates the action of the steroids testosterone and dihydrotestosterone [2].
  • Reducing equivalents that originate from NADH are transferred from ferredoxin reductase to ferredoxin and, in turn, to the terminal oxygenase, thus resulting in the activation of a dioxygen [4].
  • Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase [4].

Physical interactions of FDXR


Enzymatic interactions of FDXR

  • Under anaerobic conditions, the endogenous rate of O2 reduction by NADPH catalyzed by ferredoxin reductase (0.12 s-1 at pH 7.4) is augmented by the anthracyclines and 7-deoxyanthracyclinones [18].

Regulatory relationships of FDXR


Other interactions of FDXR


Analytical, diagnostic and therapeutic context of FDXR


  1. Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc. Coghlan, V.M., Vickery, L.E. J. Biol. Chem. (1991) [Pubmed]
  2. Structural dynamics of the human androgen receptor: implications for prostate cancer and neurodegenerative disease. Duff, J., Davies, P., Watt, K., McEwan, I.J. Biochem. Soc. Trans. (2006) [Pubmed]
  3. Male fertility is compatible with an Arg(840)Cys substitution in the AR in a large Chinese family affected with divergent phenotypes of AR insensitivity syndrome. Chu, J., Zhang, R., Zhao, Z., Zou, W., Han, Y., Qi, Q., Zhang, H., Wang, J.C., Tao, S., Liu, X., Luo, Z. J. Clin. Endocrinol. Metab. (2002) [Pubmed]
  4. Crystal structure of NADH-dependent ferredoxin reductase component in biphenyl dioxygenase. Senda, T., Yamada, T., Sakurai, N., Kubota, M., Nishizaki, T., Masai, E., Fukuda, M., Mitsuidagger, Y. J. Mol. Biol. (2000) [Pubmed]
  5. Structure-function studies of [2Fe-2S] ferredoxins. Holden, H.M., Jacobson, B.L., Hurley, J.K., Tollin, G., Oh, B.H., Skjeldal, L., Chae, Y.K., Cheng, H., Xia, B., Markley, J.L. J. Bioenerg. Biomembr. (1994) [Pubmed]
  6. Ferredoxin reductase affects p53-dependent, 5-fluorouracil-induced apoptosis in colorectal cancer cells. Hwang, P.M., Bunz, F., Yu, J., Rago, C., Chan, T.A., Murphy, M.P., Kelso, G.F., Smith, R.A., Kinzler, K.W., Vogelstein, B. Nat. Med. (2001) [Pubmed]
  7. Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Srivastava, S.K., Ramana, K.V., Bhatnagar, A. Endocr. Rev. (2005) [Pubmed]
  8. Mass spectrometric characterization of the human androgen receptor ligand-binding domain expressed in Escherichia coli. Zhu, Z., Becklin, R.R., Desiderio, D.M., Dalton, J.T. Biochemistry (2001) [Pubmed]
  9. Aldose reductase inhibitors from the nature. Kawanishi, K., Ueda, H., Moriyasu, M. Current medicinal chemistry. (2003) [Pubmed]
  10. The effect of hypertonicity on aldose reductase, alpha B-crystallin, and organic osmolytes in the retinal pigment epithelium. Lin, L.R., Carper, D., Yokoyama, T., Reddy, V.N. Invest. Ophthalmol. Vis. Sci. (1993) [Pubmed]
  11. Fibrates inhibit aldose reductase activity in the forward and reverse reactions. Balendiran, G.K., Rajkumar, B. Biochem. Pharmacol. (2005) [Pubmed]
  12. Gene expression of ferredoxin reductase predicts outcome in patients with metastatic colorectal cancer treated by 5-fluorouracil plus leucovorin. Ichikawa, W., Ooyama, A., Toda, E., Sugimoto, Y., Oka, T., Takahashi, T., Shimizu, M., Sasaki, Y., Hirayama, R. Cancer Chemother. Pharmacol. (2006) [Pubmed]
  13. The ferredoxin reductase gene is regulated by the p53 family and sensitizes cells to oxidative stress-induced apoptosis. Liu, G., Chen, X. Oncogene (2002) [Pubmed]
  14. Cloning and sequence of the human adrenodoxin reductase gene. Lin, D., Shi, Y.F., Miller, W.L. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  15. Placental cytochrome P450scc (CYP11A1): comparison of catalytic properties between conditions of limiting and saturating adrenodoxin reductase. Tuckey, R.C., Headlam, M.J. J. Steroid Biochem. Mol. Biol. (2002) [Pubmed]
  16. Development and characterization of a conditionally immortalized human osteoblastic cell line stably transfected with the human androgen receptor gene. Hofbauer, L.C., Hicok, K.C., Schroeder, M.J., Harris, S.A., Robinson, J.A., Khosla, S. J. Cell. Biochem. (1997) [Pubmed]
  17. Glucose-specific regulation of aldose reductase in capan-1 human pancreatic duct cells In vitro. Busik, J.V., Hootman, S.R., Greenidge, C.A., Henry, D.N. J. Clin. Invest. (1997) [Pubmed]
  18. Anthracycline antibiotic reduction by spinach ferredoxin-NADP+ reductase and ferredoxin. Fisher, J., Abdella, B.R., McLane, K.E. Biochemistry (1985) [Pubmed]
  19. 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. Sparkes, R.S., Klisak, I., Miller, W.L. DNA Cell Biol. (1991) [Pubmed]
  20. Human skin is a steroidogenic tissue: steroidogenic enzymes and cofactors are expressed in epidermis, normal sebocytes, and an immortalized sebocyte cell line (SEB-1). Thiboutot, D., Jabara, S., McAllister, J.M., Sivarajah, A., Gilliland, K., Cong, Z., Clawson, G. J. Invest. Dermatol. (2003) [Pubmed]
  21. Adrenodoxin: structure, stability, and electron transfer properties. Grinberg, A.V., Hannemann, F., Schiffler, B., Müller, J., Heinemann, U., Bernhardt, R. Proteins (2000) [Pubmed]
  22. Human adrenodoxin reductase: two mRNAs encoded by a single gene on chromosome 17cen----q25 are expressed in steroidogenic tissues. Solish, S.B., Picado-Leonard, J., Morel, Y., Kuhn, R.W., Mohandas, T.K., Hanukoglu, I., Miller, W.L. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  23. Ferredoxin reductase: pharmacogenomic assessment in colorectal cancer. Yu, J., Marsh, S., Ahluwalia, R., McLeod, H.L. Cancer Res. (2003) [Pubmed]
  24. Construction of a P450c27 fusion enzyme: a useful tool for analysis of vitamin D3 25-hydroxylase activity. Dilworth, F.J., Black, S.M., Guo, Y.D., Miller, W.L., Jones, G. Biochem. J. (1996) [Pubmed]
WikiGenes - Universities