Structural studies of [Fe₃S₄] and [Fe₄S₄] ferredoxins

Last modified: Wed Apr 14 12:17:39 BST 2004

[Fe₃S₄] ferredoxins

[Fe₄S₄] ferredoxins

2[Fe₄S₄] ferredoxins

7Fe ferredoxins

Polyferredoxins

[Fe₃S₄] ferredoxins

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• Duderstadt, R.E., Staples, C.R., Brereton, P.S., Adams, M.W.W. and Johnson, M.K. (1999) Effects of mutations in aspartate 14 on the spectroscopic properties of the [Fe₃S₄]^+,0 clusters in Pyrococcus furiosus ferredoxin. Biochemistry 38, 10585-10593.
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  [Fe₄S₄] ferredoxins

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  2×[Fe₄S₄] ferredoxins

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• Phillips, W.D., McDonald, C.C., Stombaugh, N.A. and Orme-Jonhson, W.H. (1974) Proton magnetic resonance and magnetic susceptibility characterization of ferredoxin I from Bacillus polymyxa. Proc. Natl. Acad. Sci. USA 71, 140-143.
• Quinkal, I., Davasse, V., Gaillard, J. and Moulis, J.-M. (1994) On the role of conserved proline residues in the structure and function of Clostridium pasteurianum 2[4Fe-4S] ferredoxin. Protein Engineering 7, 681-687.
• Reyntjens, B., Jollie, D.R., Stephens, P.J., Gao-Sheridan, H.S. and Burgess, B.K. (1997) Purification and characterization of a fixABCX-linked 2[4Fe-4S] ferredoxin from Azotobacter vinelandii. J. Biol. Inorg. Chem. 2, 595-602.
• Saeki, K., Jain, M.K., Shen, G.J., Prince, R.C. and Zeikus, J.G. (1989) Purification and properties of ferredoxin and rubredoxin from Butyribacterium methylotrophicum. J. Bacteriol. 171, 4736-4741.
• Saeki, K., Tokuda, K.-i., Fukuyama, K., Matsubara, H., Nadanami, K., Go, M. and Itoh, S. (1996) Site-specific mutagenesis of Rhodobacter capsulatus ferredoxin I, FdxN, that functions in nitrogen fixation. Role of extra residues. J. Biol. Chem. 271, 31399-31406.
• Scrofani, S.D., Brereton, P.S., Hamer, A.M., Lavery, M.J., McDowall, S.G., Vincent, G.A., Brownlee, R.T., Hoogenraad, N.J., Sadek, M. and Wedd, A.G. (1994) Comparison of native and mutant proteins provides a sequence-specific assignment of the cysteinyl ligand proton NMR resonances in the 2[Fe₄S₄] ferredoxin from Clostridium pasteurianum. Biochemistry 33, 14486-14495.
• Thompson, C.L., Johnson, C.E., Dickson, D.P.E., Cammack, R., Hall, D.O., Weser, U. and Rao, K.K. (1974) Mössbauer effect in the eight-iron ferredoxin from Clostridium pasteurianum. Evidence for the state of the iron atoms. Biochem. J. 139, 97-103.
• TranQui, D. and Jesior, J.C. (1995) Structure of the ferredoxin from Clostridium acidurici: Model at 1.8 Å resolution. Acta Crystallogr. D51, 155-159.
• Tsukihara, T., Homma, K., Fukuyama, K., Katsube, Y., Hase, T., Matsubara, H., Tanaka, N. and Kakudo, M. (1981) Preliminary X-ray diffraction studies on a [4Fe-4S] ferredoxin from Bacillus thermoproteolyticus. J. Mol. Biol. 152, 821-823.
• Yakunin, A.F., Hallenbeck, P.C., Troshina, O.Yu. and Gogotov, I.N. (1993) Purification and properties of a bacterial-type ferredoxin from the nitrogen-fixing cyanobacterium Anabaena variabilis ATCC 29413. Biochim. Biophys. Acta 1163, 124-130.

  [Fe₃S₄]+[Fe₄S₄] (7Fe) ferredoxins

• Aono, S., Bertini, I., Cowan, J.A., Luchinat, C., Rosato, A. and Viezzoli, M.S. (1996) ¹H NMR studies of the Fe₇S₈ ferredoxin from Bacillus schlegelii: A further attempt to understand Fe₃S₄ clusters. J. Biol. Inorg. Chem. 1, 523-528.
• Aono, S., Bentrop, D., Bertini, I., Donaire, A., Luchinat, C., Niikura, Y. and Rosato, A. (1998) Solution structure of the oxidized Fe₇S₈ ferredoxin from the thermophilic bacterium Bacillus schlegelii by ¹H NMR spectroscopy. Biochemistry 37, 9812-9826.
• Armengaud, J., Gaillard, J., Forest, E. and Jouanneau, Y. (1995) Characterization of a 2[4Fe-4S] ferredoxin obtained by chemical insertion of the Fe-S clusters into the apoferredoxin II from Rhodobacter capsulatus. Eur. J. Biochem. 231, 396-404.
• Armstrong, F.A., George, S.J., Cammack, R., Hatchikian, E.C. and Thomson, A.J. (1989) Electrochemical and spectroscopic characterization of the 7Fe form of ferredoxin III from Desulfovibrio africanus. Biochem. J. 264, 265-273.
• Battistuzzi, G., Borsari, M., Ferretti, S., Luchinat, C. and Sola, M. (1995) Magnetic resonance of Fe-S clusters: Isolation and characterization of a 7Fe ferredoxin from Rhodopseudomonas palustris. Arch. Biochem. Biophys. 320, 149-154.
• Bentrop, D., Bertini, I., Luchinat, C., Mendes, J., Piccioli, M. and Teixeira, M. (1996) Paramagnetic NMR analysis of the seven-iron ferredoxin from the hyperthermoacidophilic archaeon Desulfurolobus ambivalens reveals structural similarity to other dicluster ferredoxins. Eur. J. Biochem. 236, 92-99.
• Bertini, I., Dikiy, A., Luchinat, C., Macinai, R., Viezzoli, M.S. and Vincenzini, M. (1997) An NMR study of the 7Fe-8S ferredoxin from Rhodopseudomonas palustris and reinterpretation of data on similar systems. Biochemistry 36, 3570-3579.
• Bertini, I., Luchinat, C., Mincione, G. and Soriano, A. (1998) ²H NMR investigation of [Fe₃S₄]⁰ cluster in 7Fe8S ferredoxin from Bacillus schlegelii. Inorg. Chem. 37, 969-972.
• Bertini, I., Luchinat, C., Niikura, Y. and Presenti, C. (2000) Model-free analysis of a thermophilic Fe₇S₈ protein compared with a mesophilic Fe₄S₄ protein. Proteins 41, 75-85.
• Breton, J.L.J., Duff, J.L.C., Butt, J.N., Armstrong, F.A., George, S.J., Petillot, Y., Forest, E., Schafer, G. and Thomson, A.J. (1995) Identification of the iron-sulfur clusters in a ferredoxin from the archaeon Sulfolobus acidocaldarius. Evidence for a reduced [3Fe-4S] cluster with pH-dependent electronic properties. Eur. J. Biochem. 233, 937-946.
• Butt, J.N., Fawcett, S.E.J., Breton, J., Thomson, A.J. and Armstrong, F.A. (1997) Electrochemical potential and pH dependences of [3Fe-4S][M3Fe-4S] cluster transformations (M = Fe, Zn, Co, and Cd) in ferredoxin III from Desulfovibrio africanus and detection of a cluster with M = Pb. J. Am. Chem. Soc. 119, 9729-9737.
• Cheng, H., Grohmann, K. and Sweeney, W. (1990) The downfield resonances in the ¹H NMR spectra of Azotobacter vinelandii and Pseudomonas putida seven-iron ferredoxins. J. Biol. Chem. 265, 12388-12392.
• Fujii, T., Moriyama, H., Takenaka, A., Tanaka, N., Wakagi, T. and Oshima, T. (1991) Crystallization and preliminary X-ray studies on Sulfolobus acidocaldarius ferredoxin. J. Biochem. (Tokyo) 110, 472-473.
• Fujii, T., Hata, Y., Wakagi, T., Tanaka, N. and Oshima, T. (1996) Novel zinc-binding centre in thermoacidophilic archaeal ferredoxins. Nature Struct. Biol. 3, 834-837.
• Fujii, T., Hata, Y., Oozeki, M., Moriyama, H., Wakagi, T., Tanaka, N. and Oshima, T. (1997) The crystal structure of zinc-containing ferredoxin from the thermoacidophilic archaeon Sulfolobus sp. strain 7. Biochemistry 36, 1505-1513.
• Gao-Sheridan, H.S., Kemper, M.A., Khayat, R., Tilley, G.J., Armstrong, F.A., Sridhar, V., Prasad, G.S., Stout, C.D. and Burgess, B.K. (1998) A T14C variant of Azotobacter vinelandii ferredoxin I undergoes facile [3Fe-4S]⁰ to [4Fe-4S]²⁺ conversion in vitro but not in vivo. J. Biol. Chem. 273, 33692-33701.
• George, S.J., Armstrong, F.A., Hatchikian, E.C. and Thomson, A.J. (1989) Electrochemical and spectroscopic characterization of the conversion of the 7Fe into the 8Fe form of ferredoxin III from Desulfovibrio africanus. Identification of a [4Fe-4S] cluster with one non-cysteine ligand. Biochem. J. 264, 275-284.
• Ghosh, D., Furey, W., Jr., O'Donnell, S. and Stout, C.D. (1981) Structure of a 7Fe ferredoxin from Azotobacter vinelandii. J. Biol. Chem. 256, 4185-4192.
• Ghosh, D., O'Donnell, S., Furey, W., Jr., Robbins, A.H. and Stout, C.D. (1982) Iron-sulfur clusters and protein structure of Azotobacter ferredoxin at 2.0 Å resolution. J. Mol. Biol. 158, 73-109.
• Gomes, C.M., Faria, A., Carita, J.C., Mendes, J., Regalla, M., Chicau, P., Huber, H., Stetter, K.O. and Teixeira, M. (1998) Di-cluster, seven-iron ferredoxins from hyperthermophilic Sulfolobales. J. Biol. Inorg. Chem. 3, 499-507.
• Hannan, J.P., Busch, J.L.H., Breton, J., James, R., Thomson, A.J., Moore, G.R. and Davy, S.L. (2000) Characterisation of oxidised 7Fe dicluster ferredoxins with NMR spectroscopy. J. Biol. Inorg. Chem. 5, 432-447.
• Hille, R., Yoshida, T., Tarr, G.E., Williams, C.H., Ludwig, M.L., Fee, J.A., Kent, T.A., Huynh, B.-H. and Münck, E. (1983) Studies of the ferredoxin from Thermus thermophilus. J. Biol. Chem. 258, 13008-13013.
• Hirst, J., Duff, J.L.C., Jameson, G.N.L., Kemper, M.A., Burgess, B.K. and Armstrong, F.A. (1998a) Kinetics and mechanism of redox-coupled, long-range proton transfer in an iron-sulfur protein. Investigation by fast-scan protein-film voltammetry. J. Am. Chem. Soc. 120, 7085-7094 [published erratum J. Am. Chem. Soc. 120, 13284 (1998)].
• Hirst, J., Jameson, G.N.L., Allen, J.W.A. and Armstrong, F.A. (1998b) Very rapid, cooperative two-electron/two-proton redox reactions of [3Fe-4S] clusters: Detection and analysis by protein-film voltammetry. J. Am. Chem. Soc. 120, 11994-11999.
• Howard, J.B., Lorsbach, T.W., Ghosh, D., Melis, K. and Stout, C.D. (1983) Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino acid sequence and electron density maps of residues. J. Biol. Chem. 258, 508-522.
• Hu, Z., Jollie, D., Burgess, B.K., Stephens, P.J. and Münck, E. (1994) Mössbauer and EPR studies of Azotobacter vinelandii ferredoxin I. Biochemistry 33, 14475-14485.
• Imai, T., Kamata, K., Sato, T., Saito, H., Tobari, J., Ohmori, D. and Nagayama, K. (1986) Resonance Raman spectroscopic studies of 7Fe ferredoxins. In Matsubara, H., Katsube, Y. and Wada, K., Eds. Iron-sulfur protein research. Japan Scientific Societies Press, Tokyo / Springer, Berlin, pp. 109-115.
• Iwasaki, T., Wakagi, T., Isogai, Y., Tanaka, K., Iizuka, T. and Oshima, T. (1994) Functional and evolutionary implications of a [3Fe-4S] cluster of the dicluster-type ferredoxin from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. J. Biol. Chem. 269, 29444-29450.
• Johnson, M.K., Hare, J.W., Spiro, T.G., Moura, J.J.G., Xavier, A.V. and LeGall, J. (1981) Resonance Raman spectra of three-iron centers in ferredoxins from Desulfovibrio gigas. J. Biol. Chem. 256, 9806-9808.
• Johnson, M.K., Bennett, D.E., Fee, J.A. and Sweeney, W.V. (1987) Spectroscopic studies of the seven-iron-containing ferredoxins from Azotobacter vinelandii and Thermus thermophilus. Biochim. Biophys. Acta 911, 81-94.
• Jouanneau, Y., Meyer, C., Gaillard, J. and Vignais, P.M. (1990) Purification and characterization of a 7Fe-ferredoxin from Rhodobacter capsulatus. Biochem. Biophys. Res. Commun. 171, 273-279.
• Jung, Y.-S., Roberts, V.A., Stout, C.D. and Burgess, B.K. (1999) Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase. J. Biol. Chem. 274, 2978-2987.
• Kemper, M.A., Gao-Sheridan, H.S., Shen, B., Duff, J.L.C., Tilley, G.J., Armstrong, F.A. and Burgess, B.K. (1998) T14/D15 Azotobacter vinelandii ferredoxin I: Creation of a new CysXXCysXXCys motif that ligates a [4Fe-4S] cluster. Biochemistry 37, 12829-12837.
• Kojoh, K., Matsuzawa, H. and Wakagi, T. (1999) Zinc and an N-terminal extra stretch of the ferredoxin from a thermoacidophilic archaeon stabilize the molecule at high temperature. Eur. J. Biochem. 264, 85-91.
• Lutz, M., Moulis, J.-M. and Meyer, J. (1983) Resonance Raman spectroscopy of Azotobacter vinelandii ferredoxin I. Vibrational features of the [3Fe-3S] cluster. FEBS Lett. 163, 212-216.
• Macedo, A.L., Besson, S., Moreno, C., Fauque, G., Moura, J.J.G. and Moura, I. (1996) Characterization of a 7Fe ferredoxin isolated from the marine denitrifier Pseudomonas nautica strain 617: spectroscopic and electrochemical studies. Biochem. Biophys. Res. Commun. 229, 524-530.
• Martin, A.E., Burgess, B.K., Stout, C.D., Cash, V.L., Dean, D.R., Jensen, G.M. and Stephens, P.J. (1990) Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement. Proc. Natl. Acad. Sci. USA 87, 598-602.
• Merritt, E.A., Stout, G.H., Turley, S., Sieker, L.C., Jensen, L.H. and Orme-Johnson, W.H. (1993) Structure at pH 6.5 of ferredoxin I from Azotobacter vinelandii at 2.3 Å resolution. Acta Crystallogr. D49, 272-281.
• Morgan, T.V., Stephens, P.J., Devlin, F., Stout, C.D., Melis, K.A. and Burgess, B.K. (1984) Spectroscopic studies of ferricyanide oxidation of Azotobacter vinelandii ferredoxin I. Proc. Natl. Acad. Sci. USA 81, 1931-1935.
• Nagayama, K., Ohmori, D., Imai, T. and Oshima, T. (1986) NMR studies of 7Fe ferredoxins: redox states and structural changes in two iron-sulfur clusters. In Matsubara, H., Katsube, Y. and Wada, K., Eds. Iron-sulfur protein research. Japan Scientific Societies Press, Tokyo / Springer, Berlin, pp. 125-138.
• Nakajima, Y., Fujiwara, T. and Fukumori, Y. (1998) Purification and characterization of a [3Fe-4S][4Fe-4S] type ferredoxin from hyperthermophilic archaeon, Pyrobaculum islandicum. J. Biochem. (Tokyo) 123, 521-527.
• Ohmori, D., Yamakura, F., Suzuki, K., Imai, T. and Nagayama, K. (1986) Electron paramagnetic studies of 7Fe-ferredoxins, Pseudomonas ovalis and Mycobacterium smegmatis ferredoxin. In Matsubara, H., Katsube, Y. and Wada, K., Eds. Iron-sulfur protein research. Japan Scientific Societies Press, Tokyo / Springer, Berlin, pp. 116-124.
• Schipke, C.G., Goodin, D.B., McRee, D.E. and Stout, C.D. (1999) Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4 Å resolution: Conformational change of surface residues without significant change in the [3Fe-4S]^+/0 cluster. Biochemistry 38, 8228-8239.
• Shen, B., Martin, L.L., Butt, J.N., Armstrong, F.A., Stout, C.D., Jensen, G.M., Stephens, P.J., La Mar, G.N., Gorst, C.M. and Burgess, B.K. (1993) Azotobacter vinelandii ferredoxin I. Aspartate 15 facilitates proton transfer to the reduced [3Fe-4S] cluster. J. Biol. Chem. 268, 25928-25939.
• Shen, B., Jollie, D.R., Stout, C.D., Diller, T.C., Armstrong, F.A., Gorst, C.M., La Mar, G.N., Stephens, P.J. and Burgess, B.K. (1994) Azotobacter vinelandii ferredoxin I. Alteration of individual surface charges and the [4Fe-4S]^2+/+ cluster reduction potential. J. Biol. Chem. 269, 8564-8575.
• Shen, B., Jollie, D.R., Diller, T.C., Stout, C.D., Stephens, P.J. and Burgess, B.K. (1995) Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: Cysteine ligation of the [4Fe-4S] cluster with protein rearrangement is preferred over serine ligation. Proc. Natl. Acad. Sci. USA 92, 10064-10068.
• Soman, J., Iismaa, S. and Stout, C.D. (1991) Crystallographic analysis of two site-directed mutants of Azotobacter vinelandii ferredoxin. J. Biol. Chem. 266, 21558-21562.
• Sridhar, V., Prasad, G.S., Burgess, B.K. and Stout, C.D. (1998) Crystal structures of ferricyanide-oxidized [Fe-S] clusters in Azotobacter vinelandii ferredoxin I. J. Biol. Inorg. Chem. 3, 140-149.
• Stephens, P.J., Morgan, T.V., Devlin, F.J., Penner-Hahn, J.E., Hodgson, K.O., Scott, R.A., Stout, C.D. and Burgess, B.K. (1985) [4Fe-4S]-cluster-depleted Azotobacter vinelandii ferredoxin I: A new 3Fe iron-sulfur protein. Proc. Natl. Acad. Sci. USA 82, 5661-5665.
• Stephens, P.J., Jensen, G.M., Devlin, F.J., Morgan, T.V., Stout, C.D., Martin, A.E. and Burgess, B.K. (1991) Circular dichroism and magnetic circular dichroism of Azotobacter vinelandii ferredoxin I. Biochemistry 30, 3200-3209.
• Stout, C.D. (1979b) Two crystal forms of Azotobacter ferredoxin. J. Biol. Chem. 254, 3598-3599.
• Stout, C.D. (1979b) Structure of the iron-sulphur clusters in Azotobacter ferredoxin at 4.0 Å resolution. Nature 279, 83-84.
• Stout, C.D. (1988) 7-Iron ferredoxin revisited. J. Biol. Chem. 263, 9256-9260.
• Stout, C.D. (1989) Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9 Å resolution. J. Mol. Biol. 205, 545-555.
• Stout, C.D. (1993) Crystal structures of oxidized and reduced Azotobacter vinelandii ferredoxin at pH 8 and 6. J. Biol. Chem. 268, 25920-25927.
• Stout, C.D., Stura, E.A. and McRee, D.E. (1998) Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35 Å resolution and determination of the [Fe-S] bonds with 0.01 Å accuracy. J. Mol. Biol. 278, 629-639.
• Stout, G.H., Ghosh, D., Pattabhi, V. and Robbins, A.H. (1980) Iron-sulfur clusters in Azotobacter ferredoxin at 2.5 Å resolution. J. Biol. Chem. 255, 1797-1800.
• Stout, G.H., Turley, S., Sieker, L.C. and Jensen, L.H. (1988) Structure of ferredoxin I from Azotobacter vinelandii. Proc. Natl. Acad. Sci. USA 85, 1020-1022.
• Thomson, A.J., Breton, J.L.J., Butt, J.N., Hatchikian, E.C. and Armstrong, F.A. (1992) Iron-sulphur clusters with labile metal ions. J. Inorg. Biochem. 47, 197-207.
• Tsukihara, T., Fukuyama, K., Wakabayashi, S., Wada, K., Matsubara, H., Kerscher, L. and Oesterhelt, D. (1985) Preliminary X-ray diffraction studies on a ferredoxin from the thermophilic archaebacterium, Thermoplasma acidophilum. J. Mol. Biol. 186, 481-482.

  Polyferredoxins

• Hedderich, R., Albracht, S.P.J., Linder, D., Koch, J. and Thauer, R.K. (1992) Isolation and characterization of polyferredoxin from Methanobacterium thermoautotrophicum. The mvhB gene product of the methylviologen-reducing hydrogenase operon. FEBS Lett. 298, 65-68.

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