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Last modified: 16 April 1999

Bibliography on structural studies of adrenodoxin­type ferredoxins

  1. Beckert, V., Schrauber, H., Bernhardt, R., van Dijk, A.A., Kakoschke, C. and Wray, V. (1995) Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications. Eur. J. Biochem. 231, 226-235.
  2. Benson, D.E., Suslick, K.S. and Sligar, S.G. (1997) Reduced oxy intermediate observed in D251N cytochrome P450cam. Biochemistry 36, 5104-5107.
  3. Cammack, R., Rao, K.K., Hall, D.O. and Johnson, C.E. (1971) Mössbauer studies of adrenodoxin. The mechanism of electron transfer in a hydroxylase iron-sulphur protein. Biochem. J. 125, 849-856.
  4. Cooke, R., Tsibris, J.C., Debrunner, P.G., Tsai, R., Gunsalus, I.C. and Frauenfelder, H. (1968) Mössbauer studies on putidaredoxin. Proc. Natl. Acad. Sci. USA 59, 1042-1052.
  5. Fu, W., Drozdzewski, P.M., Davies, M.D., Sligar, S.G. and Johnson, M.K. (1992) Resonance Raman and magnetic circular dichroism studies of reduced [2Fe-2S] proteins. J. Biol. Chem. 267, 15502-15510.
  6. Greenfield, N.J., Wu, X.H. and Jordan, F. (1989) Proton magnetic resonance spectra of adrenodoxin: Features of the aromatic region. Biochim. Biophys. Acta 995, 246-254.
  7. Grinberg, A.V. and Bernhardt, R. (1998) Effect of replacing a conserved proline residue on the function and stability of bovine adrenodoxin. Protein Engineering 11, 1057-1064.
  8. Kazanis, S. and Pochapsky, T.C. (1997) Structural features of the metal binding site and dynamics of gallium putidaredoxin, a diamagnetic derivative of a Cys4Fe2S2 ferredoxin. J. Biomol. NMR 9, 337-346.
  9. Kulkoski, J.A. and Ghazarian, J.G. (1979) Purification and characterization of the ferredoxin component of 25­hydroxycholecalciferol 1alpha­hydroxylase. Biochem. J. 177, 673-678.
  10. Lapko, A.G. and Ruckpaul, K. (1996) Crystallization of a covalently-linked complex of adrenodoxin and adrenodoxin reductase. Biokhimiia (Moscow) 61, 1637-1647.
  11. Lapko, A.G., Müller, A., Heese, O., Ruckpaul, K. and Heinemann, U. (1997) Preparation and crystallization of a cross­linked complex of bovine adrenodoxin and adrenodoxin reductase. Proteins 28, 289-292.
  12. Lyons, T.A., Ratnaswamy, G. and Pochapsky, T.C. (1996) Redox­dependent dynamics of putidaredoxin characterized by amide proton exchange. Protein Science 5, 627-639.
  13. Marg, A., Kuban, R.J., Behlke, J., Dettmer, R. and Ruckpaul, K. (1992) Crystallization and X­ray examination of bovine adrenodoxin. J. Mol. Biol. 227, 945-947.
  14. Mino, Y., Loehr, T.M., Wada, K., Matsubara, H. and Sanders­Loehr, J. (1987) Hydrogen bonding of sulfur ligands in blue copper and iron-sulfur proteins: detection by resonance Raman spectroscopy. Biochemistry 26, 8059-8065.
  15. Miura, S. and Ichikawa, Y. (1991a) Conformational change of adrenodoxin induced by reduction of iron-sulfur cluster. Proton nuclear magnetic resonance study. J. Biol. Chem. 266, 6252-6258.
  16. Miura, S. and Ichikawa, Y. (1991b) Proton nuclear magnetic resonance investigation of adrenodoxin. Assignment of aromatic resonances and evidence for a conformational similarity with ferredoxin from Spirulina platensis. Eur. J. Biochem. 197, 747-757.
  17. Miura, S. and Ichikawa, Y. (1994) Interaction of NADPH-adrenoferredoxin reductase with NADP+ and adrenoferredoxin. Equilibrium and dynamic properties investigated by proton nuclear magnetic resonance. J. Biol. Chem. 269, 8001-8006.
  18. Moleski, C., Moss, T.H., Orme­Johnson, W.H. and Tsibris, J.C. (1970) The magnetic susceptibility of the oxidized and reduced iron-sulfur proteins adrenodoxin and putidaredoxin. Biochim. Biophys. Acta 214, 548-550.
  19. Müller, A., Müller, J.J., Müller, Y.A., Uhlmann, H., Bernhardt, R. and Heinemann, U. (1998) New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108). Structure 6, 269-280.
  20. Pedersen, J.I., Ghazarian, J.G., Orme­Johnson, N.R. and DeLuca, H.F. (1976) Isolation of chick renal mitochondrial ferredoxin active in the 25­hydroxyvitamin D3­1alpha­hydroxylase system. J. Biol. Chem. 251, 3933-3941.
  21. Pochapsky, T.C. and Ye, X.M. (1991) 1H NMR identification of a ß­sheet structure and description of folding topology in putidaredoxin. Biochemistry 30, 3850-3856.
  22. Pochapsky, T.C., Ratnaswamy, G. and Patera, A. (1994a) Redox­dependent 1H NMR spectral features and tertiary structural constraints on the C­terminal region of putidaredoxin. Biochemistry 33, 6433-6441.
  23. Pochapsky, T.C., Ye, X.M., Ratnaswamy, G. and Lyons, T.A. (1994b) An NMR­derived model for the solution structure of oxidized putidaredoxin, a 2­Fe, 2­S ferredoxin from Pseudomonas. Biochemistry 33, 6424-6432.
  24. Pochapsky, T.C., Jain, N.U., Kuti, M., Lyons, T.A. and Heymont, J. (1999) A refined model for the solution structure of oxidized putidaredoxin. Biochemistry 38, 4681-4690. [Electronic Supplementary Material]
  25. Ratnaswamy, G. and Pochapsky, T.C. (1993) Characterization of hyperfine­shifted 1H resonances in oxidized and reduced putidaredoxin, an Fe2S2 ferredoxin from Pseudomonas putida. Magn. Reson. Chem. 31, S73-S77.
  26. Sakamoto, H., Ichikawa, Y., Yamano, T. and Takagi, T. (1981) Circular dichroic studies on the interaction between reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase and adrenodoxin. J. Biochem. (Tokyo) 90, 1445-1452.
  27. Shimada, H., Nagano, S., Ariga, Y., Unno, M., Egawa, T., Hishiki, T., Ishimura, Y., Masuya, F., Obata, T. and Hori, H. (1999) Putidaredoxin-cytochrome P450cam interaction. Spin state of the heme iron modulates putidaredoxin structure. J. Biol. Chem. 274, 9363-9369.
  28. Skjeldal, L., Markley, J.L., Coghlan, V.M. and Vickery, L.E. (1991) 1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins. Biochemistry 30, 9078-9083.
  29. Sugiura, Y., Ishizu, K. and Kimura, T. (1974) A rubredoxin­like mononuclear FeS4 derivative of adrenal iron-sulfur protein (adrenodoxin). Biochem. Biophys. Res. Commun. 60, 334-340.
  30. Sugiura, Y., Ishizu, K. and Kimura, T. (1975) Cobalt and ruthenium replacement for iron in adrenal iron-sulfur protein (adrenodoxin). Preparation and some properties. Biochemistry 14, 97-101.
  31. Unno, M., Christian, J.F., Benson, D.E., Gerber, N.C., Sligar, S.G. and Champion, P.M. (1997) Resonance Raman investigations of cytochrome P450cam complexed with putidaredoxin. J. Am. Chem. Soc. 119, 6614-6620.
  32. Vidakovic, M.S., Fraczkiewicz, G. and Germanas, J.P. (1996) Expression and spectroscopic characterization of the hydrogenosomal [2Fe-2S] ferredoxin from the protozoan Trichomonas vaginalis. J. Biol. Chem. 271, 14734-14739.
  33. Xia, B., Cheng, H., Skjeldal, L., Coghlan, V.M., Vickery, L.E. and Markley, J.L. (1995) Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin. Biochemistry 34, 180-187.
  34. Xia, B., Cheng, H., Bandarian, V., Reed, G.H. and Markley, J.L. (1996) Human ferredoxin: overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine­to­serine mutants. Biochemistry 35, 9488-9495.
  35. Xia, B., Volkman, B.F. and Markley, J.L. (1998) Evidence for oxidation­state­dependent conformational changes in human ferredoxin from multinuclear, multidimensional NMR spectroscopy. Biochemistry 37, 3965-3973.
  36. Ye, X.M., Pochapsky, T.C. and Pochapsky, S.S. (1992) 1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron­transfer protein from Pseudomonas. Biochemistry 31, 1961-1968.