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FDXR  -  ferredoxin reductase

Bos taurus

Synonyms: AR, AdR
 
 
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Disease relevance of FDXR

  • Mutant proteins were expressed in Escherichia coli and were assayed for activity by ferredoxin-mediated electron transfer to cytochrome c. Replacement of Lys-242 (homologous to Lys-243 in bovine Fd-reductase) with Gln and replacement of Arg-241 with Ser had little effect (2.7- and 3.6-fold increased Km, respectively) [1].
  • Two cDNAs (differing by the presence or absence of an 18-bp insert in the coding region) for the human Fd-reductase were subcloned into a newly constructed general purpose expression vector, p delta blue; protein expression under control of the bacteriophage lambda pL promoter was then induced in Escherichia coli [2].
  • Here we analyzed the interaction between bovine adrenodoxin reductase and flavodoxin from the cyanobacterium Anabaena PCC 7119 [3].
 

High impact information on FDXR

  • These P450s receive electrons from NADPH via adrenodoxin reductase and adrenodoxin [4].
  • In addition, variation of the ionic strength in these experiments revealed different optimum salt concentrations for the reduction of adrenodoxin reductase and adrenodoxin, respectively, and unraveled dramatically changing reduction rates of CYP11A1 by adrenodoxin [5].
  • In conclusion, increased AR activity contributes to retinal oxidative stress and VEGF protein overexpression in early diabetes [6].
  • The steroid hydroxylating system of adrenal cortex mitochondria consists of the membrane-attached NADPH-dependent adrenodoxin reductase (AR), the soluble one-electron transport protein adrenodoxin (Adx), and a membrane-integrated cytochrome P450 of the CYP11 family [7].
  • The [2Fe-2S] cluster of Adx and the isoalloxazine rings of FAD of AR are 10 A apart suggesting a possible electron transfer route between these redox centers [7].
 

Biological context of FDXR

 

Anatomical context of FDXR

 

Associations of FDXR with chemical compounds

  • NADPH ferredoxin reductase and ferredoxin also catalyzed NADPH-dependent deiodination of L-diiodotyrosine; bovine adrenodoxin and adrenodoxin reductase could partially replace the thyroidal components in NADPH-dependent deiodination of L-diiodotyrosine [12].
  • Adrenodoxin reductase receives a two-electron package from NADPH and converts it to two single electrons that are transferred via adrenodoxin to all mitochondrial cytochromes P 450 [8].
  • The three reported structures of adrenodoxin reductase were ligated with reduced and oxidized NADP and have now confirmed this equivalence also for the NADP-binding site [16].
  • Treatment of adrenodoxin reductase with a highly purified preparation of neuraminidase demonstrates that neither the adrenodoxin-independent ferricyanide reductase activity nor the adrenodoxin-dependent cytochrome c reductase activity of the enzyme is affected by neuraminidase treatment [17].
  • Covalent crosslinking experiments using a water-soluble carbodiimide show that adrenodoxin crosslinks exclusively to the 30.6 kDa fragment, thus implicating the N-terminal region of adrenodoxin reductase in binding to the iron-sulfur protein [17].
 

Physical interactions of FDXR

 

Enzymatic interactions of FDXR

 

Other interactions of FDXR

 

Analytical, diagnostic and therapeutic context of FDXR

References

  1. Charge pair interactions stabilizing ferredoxin-ferredoxin reductase complexes. Identification by complementary site-specific mutations. Brandt, M.E., Vickery, L.E. J. Biol. Chem. (1993) [Pubmed]
  2. Expression and characterization of human mitochondrial ferredoxin reductase in Escherichia coli. Brandt, M.E., Vickery, L.E. Arch. Biochem. Biophys. (1992) [Pubmed]
  3. Analysis of the interaction of a hybrid system consisting of bovine adrenodoxin reductase and flavodoxin from the cyanobacterium Anabaena PCC 7119. Zöllner, A., Nogués, I., Heinz, A., Medina, M., Gómez-Moreno, C., Bernhardt, R. Bioelectrochemistry (Amsterdam, Netherlands) (2004) [Pubmed]
  4. Zone-specific regulation of two messenger RNAs for P450c11 in the adrenals of pregnant and nonpregnant rats. Malee, M.P., Mellon, S.H. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  5. Stripping down the mitochondrial cholesterol hydroxylase system, a kinetics study. Schiffler, B., Zöllner, A., Bernhardt, R. J. Biol. Chem. (2004) [Pubmed]
  6. Aldose reductase inhibitor fidarestat prevents retinal oxidative stress and vascular endothelial growth factor overexpression in streptozotocin-diabetic rats. Obrosova, I.G., Minchenko, A.G., Vasupuram, R., White, L., Abatan, O.I., Kumagai, A.K., Frank, R.N., Stevens, M.J. Diabetes (2003) [Pubmed]
  7. Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis. Müller, J.J., Lapko, A., Bourenkov, G., Ruckpaul, K., Heinemann, U. J. Biol. Chem. (2001) [Pubmed]
  8. The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis. Ziegler, G.A., Vonrhein, C., Hanukoglu, I., Schulz, G.E. J. Mol. Biol. (1999) [Pubmed]
  9. Molecular cloning and sequence analysis of full-length cDNA for mRNA of adrenodoxin oxidoreductase from bovine adrenal cortex. Nonaka, Y., Murakami, H., Yabusaki, Y., Kuramitsu, S., Kagamiyama, H., Yamano, T., Okamoto, M. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
  10. cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases. Hanukoglu, I., Gutfinger, T. Eur. J. Biochem. (1989) [Pubmed]
  11. Design of an Escherichia coli system for whole cell mediated steroid synthesis and molecular evolution of steroid hydroxylases. Hannemann, F., Virus, C., Bernhardt, R. J. Biotechnol. (2006) [Pubmed]
  12. Ferredoxin and ferredoxin reductase activities in bovine thyroid. Possible relationship to iodotyrosine deiodinase. Goswami, A., Rosenberg, I.N. J. Biol. Chem. (1981) [Pubmed]
  13. Isolation of chick renal mitochondrial ferredoxin active in the 25-hydroxyvitamin D3-1alpha-hydroxylase system. Pedersen, J.I., Ghazarian, J.G., Orme-Johnson, N.R., DeLuca, H.F. J. Biol. Chem. (1976) [Pubmed]
  14. Vertebrate-type and plant-type ferredoxins: crystal structure comparison and electron transfer pathway modelling. Müller, J.J., Müller, A., Rottmann, M., Bernhardt, R., Heinemann, U. J. Mol. Biol. (1999) [Pubmed]
  15. cDNA cloning of mouse ferredoxin reductase from kidney. Itoh, S., Iemura, O., Yamada, E., Yoshimura, T., Tsujikawa, K., Kohama, Y., Mimura, T. Biochim. Biophys. Acta (1995) [Pubmed]
  16. Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family. Ziegler, G.A., Schulz, G.E. Biochemistry (2000) [Pubmed]
  17. Structural and functional characterization of bovine adrenodoxin reductase by limited proteolysis. Warburton, R.J., Seybert, D.W. Biochim. Biophys. Acta (1995) [Pubmed]
  18. C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450. Uhlmann, H., Kraft, R., Bernhardt, R. J. Biol. Chem. (1994) [Pubmed]
  19. 3-Methoxybenzidine: a potent inhibitor of cholesterol side chain cleavage cytochrome P-450. Duval, J.F., Vickery, L.E. Steroids (1980) [Pubmed]
  20. Properties of ferredoxin reductase and ferredoxin from the bovine corpus luteum. Tuckey, R.C., Stevenson, P.M. Int. J. Biochem. (1984) [Pubmed]
  21. The loop region covering the iron-sulfur cluster in bovine adrenodoxin comprises a new interaction site for redox partners. Hannemann, F., Rottmann, M., Schiffler, B., Zapp, J., Bernhardt, R. J. Biol. Chem. (2001) [Pubmed]
  22. Cobalt and ruthenium replacement for iron in adrenal iron-sulfur protein (adrenodoxin). Preparation and some properties. Sugiura, Y., Ishizu, K., Kimura, T. Biochemistry (1975) [Pubmed]
  23. Stimulation by endozepine of the side-chain cleavage of cholesterol in a reconstituted enzyme system. Brown, A.S., Hall, P.F. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  24. Isolation of a cDNA for adrenodoxin reductase (ferredoxin-NADP+ reductase). Implications for mitochondrial cytochrome P-450 systems. Hanukoglu, I., Gutfinger, T., Haniu, M., Shively, J.E. Eur. J. Biochem. (1987) [Pubmed]
  25. Immunohistochemical localization of aldose reductase. I. Enzyme purification and antibody preparation--localization in peripheral nerve, artery, and testis. Ludvigson, M.A., Sorenson, R.L. Diabetes (1980) [Pubmed]
 
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