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Last modified: 12 February 1999

Bibliography on structural studies of plant­type ferredoxins

  1. Achim, C., Golinelli, M.­P., Bominaar, E.L., Meyer, J. and Münck, E. (1996) Mössbauer study of Cys56Ser mutant 2Fe ferredoxin from Clostridium pasteurianum: Evidence for double exchange in an [Fe2S2]+ cluster. J. Am. Chem. Soc. 118, 8168-8169.
  2. Aliverti, A., Hagen, W.R. and Zanetti, G. (1995) Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer properties. FEBS Lett. 368, 220-224.
  3. Anderson, R.E., Dunham, W.R., Sands, R.H., Bearden, A.J. and Crespi, H.L. (1975) On the nature of the iron sulfur cluster in a deuterated algal ferredoxin. Biochim. Biophys. Acta 408, 306-318.
  4. Atherton, N.M., Garbett, K., Gillard, R.D., Mason, R., Mayhew, S.J., Peel, J.L. and Stangroom, J.E. (1966) Spectroscopic investigation of rubredoxin and ferredoxin. Nature 212, 590-593.
  5. Baumann, B., Sticht, H., Schärpf, M., Sutter, M., Haehnel, W. and Rösch, P. (1996) Structure of Synechococcus elongatus [Fe2S2] ferredoxin in solution. Biochemistry 35, 12831-12841.
  6. Benelli, C., Gatteschi, D. and Zanchini, C. (1987) Angular­overlap analysis of the iron(II) site in [2Fe-2S] clusters. Biochim. Biophys. Acta 893, 365-371.
  7. Binda, C., Coda, A., Aliverti, A., Zanetti, G. and Mattevi, A. (1998) Structure of the mutant E92K of [2Fe-2S] ferredoxin I from Spinacia oleracea at 1.7 Å resolution. Acta Crystallogr. D54, 1353-1358.
  8. Brintzinger, H., Palmer, G. and Sands, R.H. (1966) On the ligand field of iron in ferredoxin from spinach chloroplasts and related nonheme iron enzymes. Proc. Natl. Acad. Sci. USA 55, 397-404.
  9. Cammack, R., Neumann, J., Nelson, N. and Hall, D.O. (1971) Circular dichroism studies of the complex between ferredoxin and ferredoxin-NADP reductase. Biochem. Biophys. Res. Commun. 42, 292-297.
  10. Chae, Y.K., Abildgaard, F., Mooberry, E.S. and Markley, J.L. (1994) Multinuclear, multidimensional NMR studies of Anabaena 7120 heterocyst ferredoxin. Sequence­specific resonance assignments and secondary structure of the oxidized form in solution. Biochemistry 33, 3287-3295.
  11. Chae, Y.K. and Markley, J.L. (1995) Analysis of the hyperfine­shifted nitrogen­15 resonances of the oxidized form of Anabaena 7120 heterocyst ferredoxin. Biochemistry 34, 188-193.
  12. Cheng, H., Xia, B., Reed, G.H. and Markley, J.L. (1994) Optical, EPR, and 1H NMR spectroscopy of serine­ligated [2Fe-2S] ferredoxins produced by site­directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin. Biochemistry 33, 3155-3164.
  13. Cheng, H., Westler, W.M., Xia, B., Oh, B.H. and Markley, J.L. (1995) Protein expression, selective isotopic labeling, and analysis of hyperfine­shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S] ferredoxin. Arch. Biochem. Biophys. 316, 619-634.
  14. Correll, C.C., Batie, C.J., Ballou, D.P. and Ludwig, M.L. (1985) Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomonas cepacia. J. Biol. Chem. 260, 14633-14635.
  15. Correll, C.C., Batie, C.J., Ballou, D.P. and Ludwig, M.L. (1992) Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science 258, 1604-1610.
  16. Correll, C.C., Ludwig, M.L., Bruns, C.M. and Karplus, P.A. (1993) Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin. Protein Science 2, 2112-2133.
  17. Dikanov, S.A. and Bowman, M.K. (1998) Determination of ligand conformation in reduced [2Fe-2S] ferredoxin from cysteine ß­proton hyperfine couplings. J. Biol. Inorg. Chem. 3, 18-29.
  18. Dikanov, S.A., Tyryshkin, A.M., Felli, I., Reijerse, E.J. and Huttermann, J. (1995) C­band ESEEM of strongly coupled peptide nitrogens in reduced two­iron ferredoxin. J. Magn. Reson. B108, 99-102.
  19. Dugad, L.B., La Mar, G.N., Banci, L. and Bertini, I. (1990) Identification of localized redox states in plant­type two­iron ferredoxins using the nuclear Overhauser effect. Biochemistry 29, 2263-2271.
  20. Dunham, W.R., Palmer, G., Sands, R.H. and Bearden, A.J. (1971) On the structure of the iron-sulfur complex in the two­iron ferredoxins. Biochim. Biophys. Acta 253, 373-384.
  21. Frolow, F., Harel, M., Sussman, J.L., Mevarech, M. and Shoham, M. (1996) Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin. Nature Struct. Biol. 3, 452-457.
  22. 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.
  23. Fukuyama, K., Ueki, N., Nakamura, H., Tsukihara, T. and Matsubara, H. (1995) Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 Å resolution: Structural comparisons of plant­type ferredoxins and an electrostatic potential analysis. J. Biochem. (Tokyo) 117, 1017-1023.
  24. Gayda, J.­P., Gibson, J.F., Cammack, R., Hall, D.O. and Mullinger, R. (1976) Spin lattice relaxation and exchange interaction in a 2­iron, 2­sulphur protein. Biochim. Biophys. Acta 434, 154-163.
  25. Gayda, J.­P., Bertrand, P., Deville, A., More, C., Roger, G., Gibson, J.F. and Cammack, R. (1979) Temperature dependence of the electronic spin­lattice relaxation time in a 2­iron­2­sulfur protein. Biochim. Biophys. Acta 581, 15-26.
  26. Geary, P.J., Saboowalla, F., Patil, D. and Cammack, R. (1984) An investigation of the iron-sulphur proteins of benzene dioxygenase from Pseudomonas putida by electron­spin­resonance spectroscopy. Biochem. J. 217, 667-673.
  27. Hasumi, H. (1982) Analyses of optical absorption and circular dichroism spectra of spinach ferredoxin at alkaline pH. J. Biochem. (Tokyo) 92, 1049-1057.
  28. Hatanaka, H., Tanimura, R., Katoh, S. and Inagaki, F. (1997) Solution structure of ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus and its thermostability. J. Mol. Biol. 268, 922-933.
  29. Hosein, B., Friesner, R. and Holzwarth, G. (1974) Ferredoxin circular dichroism at 3600 cm-1. Biochim. Biophys. Acta 368, 18-21.
  30. Hugo, N., Armengaud, J., Gaillard, J., Timmis, K.N. and Jouanneau, Y. (1998) A novel [2Fe-2S] ferredoxin from Pseudomonas putida mt2 promotes the reductive reactivation of catechol 2,3­dioxygenase. J. Biol. Chem. 273, 9622-9629.
  31. Hurley, J.K., Weber­Main, A.M., Stankovich, M.T., Benning, M.M., Thoden, J.B., Vanhooke, J.L., Holden, H.M., Chae, Y.K., Xia, B., Cheng, H., Markley, J.L., Martinez­Júlvez, M., Gómez­Moreno, C., Schmeits, J.L. and Tollin, G. (1997a) Structure­function relationships in Anabaena ferredoxin: Correlations between X­ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site­specific ferredoxin mutants. Biochemistry 36, 11100-11117.
  32. Hurley, J.K., Weber­Main, A.M., Hodges, A.E., Stankovich, M.T., Benning, M.M., Holden, H.M., Cheng, H., Xia, B., Markley, J.L., Genzor, C., Gómez­Moreno, C., Hafezi, R. and Tollin, G. (1997b) Iron-sulfur cluster cysteine­to­serine mutants of Anabaena [2Fe-2S] ferredoxin exhibit unexpected redox properties and are competent in electron transfer to ferredoxin:NADP+ reductase. Biochemistry 36, 15109-15117.
  33. Ikemizu, S., Bando, M., Sato, T., Morimoto, Y., Tsukihara, T. and Fukuyama, K. (1994) Structure of [2Fe-2S] ferredoxin I from Equisetum arvense at 1.8 Å resolution. Acta Crystallogr. D50, 167-174.
  34. Im, S.­c., Kohzuma, T., McFarlane, W., Gaillard, J. and Sykes, A.G. (1997) Formation, properties, and characterization of a fully reduced FeIIFeII form of spinach (and parsley) [2Fe-2S] ferredoxin with the macrocyclic complex [Cr(15­aneN4)(H2O)2]2+ as reductant. Inorg. Chem. 36, 1388-1396.
  35. Im, S.­c., Liu, G., Luchinat, C., Sykes, A.G. and Bertini, I. (1998) The solution structure of parsley [2Fe-2S]ferredoxin. Eur. J. Biochem. 258, 465-477.
  36. Jacobson, B.L., Chae, Y.K., Bohme, H., Markley, J.L. and Holden, H.M. (1992) Crystallization and preliminary analysis of oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120. Arch. Biochem. Biophys. 294, 279-281.
  37. Jacobson, B.L., Chae, Y.K., Markley, J.L., Rayment, I. and Holden, H.M. (1993) Molecular structure of the oxidized, recombinant, heterocyst [2Fe-2S] ferredoxin from Anabaena 7120 determined to 1.7­Å resolution. Biochemistry 32, 6788-6793.
  38. Johnson, C.E. and Hall, D.O. (1968) Mössbauer effect study of the state of iron in spinach ferredoxin. Nature 217, 446-448.
  39. Johnson, C.E., Cammack, R., Rao, K.K. and Hall, D.O. (1971) The interpretation of the EPR and Mössbauer spectra of two­iron, one­electron, iron-sulphur proteins. Biochem. Biophys. Res. Commun. 43, 564-571.
  40. Kunita, A., Koshibe, M., Nishkawa, Y., Fukuyama, K., Tsukihara, T., Katsube, Y., Matsuura, Y., Tanaka, N., Kakudo, M., Hase, T. and Matsubara, H. (1978) Crystallization and a 5 Å X­ray diffraction study of Aphanothece sacrum ferredoxin. J. Biochem. (Tokyo) 84, 989-992.
  41. Lelong, C., Sétif, P., Bottin, H., André, F. and Neumann, J.­M. (1995) 1H and 15N sequential assignment, secondary structure, and tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803. Biochemistry 34, 14462-14473.
  42. Mardanian, S.S., Demin, Yu.M. and Nalbandian, R.M. (1977) Fluorescent properties of b­type ferredoxins. Biokhimiia (Moscow) 42, 1024-1029.
  43. Meyer, J., Moulis, J.­M. and Lutz, M. (1984) Structural differences between [2Fe-2S] clusters in spinach ferredoxin and in the "red paramagnetic protein" from Clostridium pasteurianum. A resonance Raman study. Biochem. Biophys. Res. Commun. 119, 828-835.
  44. Meyer, J., Fujinaga, J., Gaillard, J. and Lutz, M. (1994) Mutated forms of the [2Fe-2S] ferredoxin from Clostridium pasteurianum with noncysteinyl ligands to the iron-sulfur cluster. Biochemistry 33, 13642-13650.
  45. 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.
  46. Moshiri, F., Crouse, B.R., Johnson, M.K. and Maier, R.J. (1995) The "nitrogenase­protective" FeSII protein of Azotobacter vinelandii: Overexpression, characterization, and crystallization. Biochemistry 34, 12973-12982.
  47. Ogawa ,K., Tsukihara, T., Tahara, H., Katsube, Y. and Matsuura, Y. (1977) Location of the iron-sulfur cluster in Spirulina platensis ferredoxin by x­ray analysis. J. Biochem. (Tokyo) 81, 529-531.
  48. Oh, B.­H. and Markley, J.L. (1990a) Multinuclear magnetic resonance studies of the 2Fe·2S* ferredoxin from Anabaena species strain PCC 7120. 1. Sequence­specific hydrogen­1 resonance assignments and secondary structure in solution of the oxidized form. Biochemistry 29, 3993-4004.
  49. Oh, B.­H. and Markley, J.L. (1990b) Multinuclear magnetic resonance studies of the 2Fe·2S* ferredoxin from Anabaena species strain PCC 7120. 3. Detection and characterization of hyperfine­shifted nitrogen­15 and hydrogen­1 resonances of the oxidized form. Biochemistry 29, 4012-4017.
  50. Oh, B.­H., Mooberry, E.S. and Markley, J.L. (1990) Multinuclear magnetic resonance studies of the 2Fe·2S* ferredoxin from Anabaena species strain PCC 7120. 2. Sequence­specific carbon­13 and nitrogen­15 resonance assignments of the oxidized form. Biochemistry 29, 4004-4011.
  51. Palmer, G. and Brintzinger, H. (1966) Nature of the non­haem iron in ferredoxin and rubredoxin. Nature 211, 189-190.
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  53. Palmer, G., Dunham, W.R., Fee, J.A., Sands, R.H., Iizuka, T. and Yonetani, T. (1971) The magnetic susceptibility of spinach ferredoxin from 77-250 °K: A measurement of the antiferromagnetic coupling between the two iron atoms. Biochim. Biophys. Acta 245, 201-207.
  54. Petersson, L., Cammack, R. and Rao, K.K. (1980) Antiferromagnetic exchange interaction in the two­iron­two­sulphur ferredoxin from the blue­green alga Spirulina maxima studied with a highly sensitive magnetic balance. Biochim. Biophys. Acta 622, 18-24.
  55. Rao, J.K. and Argos, P. (1981) Structural stability of halophilic proteins. Biochemistry 20, 6536-6543.
  56. Rao, K.K., Cammack, R., Hall, D.O. and Johnson, C.E. (1971) Mössbauer effect in Scenedesmus and spinach ferredoxins. The mechanism of electron transfer in plant­type iron-sulphur proteins. Biochem. J. 122, 257-265.
  57. Riedel, A., Fetzner, S., Rampp, M., Lingens, F., Liebl, U., Zimmermann, J.L. and Nitschke, W. (1985) EPR, electron spin echo envelope modulation, and electron nuclear double resonance studies of the 2Fe2S centers of the 2­halobenzoate 1,2­dioxygenase from Burkholderia (Pseudomonas) cepacia 2CBS. J. Biol. Chem. 270, 30869-30873.
  58. Rupp, H., Rao, K.K., Hall, D.O. and Cammack, R. (1978) Electron spin relaxation of iron-sulphur proteins studied by microwave power saturation. Biochim. Biophys. Acta 537, 255-260.
  59. Rypniewski, W.R., Breiter, D.R., Benning, M.M., Wesenberg, G., Oh, B.­H., Markley, J.L., Rayment, I. and Holden, H.M. (1991) Crystallization and structure determination to 2.5­Å resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120. Biochemistry 30, 4126-4131.
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  61. Skjeldal, L., Westler, W.M., Oh, B.H., Krezel, A.M., Holden, H.M., Jacobson, B.L., Rayment, I. and Markley, J.L. (1991) Two­dimensional magnetization exchange spectroscopy of Anabaena 7120 ferredoxin. Nuclear Overhauser effect and electron self­exchange cross peaks from amino acid residues surrounding the 2Fe-2S* cluster. Biochemistry 30, 7363-7268.
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  65. Thomson, A.J., Cammack, R., Hall, D.O., Rao, K.K., Briat, B., Rivoal, J.C. and Badoz, J. (1977) The low temperature magnetic circular dichroism spectra of iron-sulphur proteins. II. Two­iron ferredoxins. Biochim. Biophys. Acta 493, 132-141.
  66. Tsukihara, T., Fukuyama, K., Tahara, H., Katsube, Y., Matsuura, Y., Tanaka, N., Kakudo, M., Wada, K. and Matsubara, H. (1978) X­ray analysis of ferredoxin from Spirulina platensis. II. Chelate structure of active center. J. Biochem. (Tokyo) 84, 1645-1647.
  67. Tsukihara, T., Fukuyama, K., Nakamura, M., Katsube, Y., Tanaka, N., Kakudo, M., Wada, K., Hase, T. and Matsubara, H. (1981) X­ray analysis of a [2Fe-2S] ferrodoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5 Å resolution. J. Biochem. (Tokyo) 90, 1763-1773.
  68. Tsukihara, T., Fukuyama, K., Mizushima, M., Harioka, T., Kusunoki, M., Katsube, Y., Hase, T. and Matsubara, H. (1990) Structure of the [2Fe-2S] ferredoxin I from the blue­green alga Aphanothece sacrum at 2.2 Å resolution. J. Mol. Biol. 216, 399-410.
  69. Tsutsui, T., Tsukihara, T., Fukuyama, K., Katsube, Y., Hase, T., Matsubara, H., Nishikawa, Y. and Tanaka, N. (1983) Main chain fold of a [2Fe-2S] ferredoxin I from Aphanothece sacrum at 2.5 Å resolution. J. Biochem. (Tokyo) 94, 299-302.
  70. Vidakovic, M., Fraczkiewicz, G., Dave, B.C., Czernuszewicz, R.S. and Germanas, J.P. (1995) The environment of [2Fe-2S] clusters in ferredoxins: the role of residue 45 probed by site­directed mutagenesis. Biochemistry 34, 13906-13913.
  71. Vo, E., Wang, H.C. and Germanas, J.P. (1997) Preparation and characterization of [2Ga­2S] Anabaena 7120 ferredoxin, the first gallium­sulfur cluster­containing protein. J. Am. Chem. Soc. 119, 1934-1940.
Reviews on plant­type ferredoxins