Structural studies of [Fe₂S₂] ferredoxins

Last modified: Wed Apr 14 12:17:59 BST 2004

Adrenodoxin family

Plant-type

Adrenodoxin family [Fe₂S₂] ferredoxins

• Aoki, M., Ishimori, K. and Morishima, I. (1998a) Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in P450cam monooxygenase system. Biochim. Biophys. Acta 1386, 157-167.
• Aoki, M., Ishimori, K. and Morishima, I. (1998b) NMR studies of putidaredoxin: associations of putidaredoxin with NADH-putidaredoxin reductase and cytochrome P450cam. Biochim. Biophys. Acta 1386, 168-178.
• Armengaud, J., Gaillard, J. and Timmis, K.N. (2000) A second [2Fe-2S] ferredoxin from Sphingomonas sp. strain RW1 can function as an electron donor for the dioxin dioxygenase. J. Bacteriol. 182, 2238-2244.
• Armengaud, J., Sainz, G., Jouanneau, Y. and Sieker, L.C. (2001) Crystallization and preliminary X-ray diffraction analysis of a [2Fe-2S] ferredoxin (FdVI) from Rhodobacter capsulatus. Acta Crystallogr. D57, 301-303.
• Avila, L., Wirtz, M., Bunce, R.A. and Rivera, M. (1999) An electrochemical study of the factors responsible for modulating the reduction potential of putidaredoxin. J. Biol. Inorg. Chem. 4, 664-674.
• 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.
• Benson, D.E., Suslick, K.S. and Sligar, S.G. (1997) Reduced oxy intermediate observed in D251N cytochrome P450_cam. Biochemistry 36, 5104-5107.
• Bera, A.K., Grinberg, A. and Bernhardt, R. (1999) A step toward understanding the folding mechanism of bovine adrenodoxin. Arch. Biochem. Biophys. 361, 315-322.
• Bernhardt, R., Müller, A., Uhlmann, H., Grinberg, A., Müller, J.J. and Heinemann, U. (1998) Structure of adrenodoxin and function in mitochondrial steroid hydroxylation. Endocr. Res. 24, 531-539.
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• 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.
• Furukawa, Y. and Morishima, I. (2001) The role of water molecules in the association of cytochrome P450cam with putidaredoxin. An osmotic pressure study. J. Biol. Chem. 276, 12983-12990.
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• 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.
• Grinberg, A.V. and Bernhardt, R. (2001) Contribution of a salt bridge to the thermostability of adrenodoxin determined by site-directed mutagenesis. Arch. Biochem. Biophys. 396, 25-34.
• Iametti, S., Uhlmann, H., Ragg, E., Sala, N., Grinberg, A., Beckert, V., Bernhardt, R. and Bonomi, F. (1998) Cluster-iron substitution is related to structural and functional features of adrenodoxin mutants and to their redox states. Eur. J. Biochem. 251, 673-681.
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• Jain, N.U. and Pochapsky, T.C. (1999) A new assignment strategy for the hyperfine-shifted ¹³C and ¹⁵N resonances in Fe₂S₂ ferredoxins. Biochem. Biophys. Res. Commun. 258, 54-59.
• Jose, J., Bernhardt, R. and Hannemann, F. (2001) Functional display of active bovine adrenodoxin on the surface of E. coli by chemical incorporation of the [2Fe-2S] cluster. ChemBioChem 2, 695-701.
• Kakuta, Y., Horio, T., Takahashi, Y. and Fukuyama, K. (2001) Crystal structure of Escherichia coli Fdx, an adrenodoxin-type ferredoxin involved in the assembly of iron-sulfur clusters. Biochemistry 40, 11007-11012.
• 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.
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• Mo, H., Pochapsky, S.S. and Pochapsky, T.C. (1999) A model for the solution structure of oxidized terpredoxin, a Fe₂S₂ ferredoxin from Pseudomonas. Biochemistry 38, 5666-5675. [Supplementary Material]
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• 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.
• Müller, J.J., Lapko, A., Bourenkov, G., Ruckpaul, K. and Heinemann, U. (2001) Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis. J. Biol. Chem. 276, 2786-2789.
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• Pikuleva, I.A., Tesh, K., Waterman, M.R. and Kim, Y. (2000) The tertiary structure of full-length bovine adrenodoxin suggests functional dimers. Arch. Biochem. Biophys. 373, 44-55.
• Pochapsky, T.C. and Ye, X.M. (1991) ¹H NMR identification of a -sheet structure and description of folding topology in putidaredoxin. Biochemistry 30, 3850-3856.
• Pochapsky, T.C., Ratnaswamy, G. and Patera, A. (1994a) Redox-dependent ¹H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin. Biochemistry 33, 6433-6441.
• Pochapsky, T.C., Ye, X.M., Ratnaswamy, G. and Lyons, T.A. (1994b) An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas. Biochemistry 33, 6424-6432.
• Pochapsky, T.C., Kuti, M. and Kazanis, S. (1998) The solution structure of a gallium-substituted putidaredoxin mutant: GaPdx C85S. J. Biomol. NMR 12, 407-415.
• 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. [Supplementary Material]
• Pochapsky, T.C., Kostic, M., Jain, N. and Pejchal, R. (2001) Redox-dependent conformational selection in a Cys₄Fe₂S₂ ferredoxin. Biochemistry 40, 5602-5614.
• Ratnaswamy, G. and Pochapsky, T.C. (1993) Characterization of hyperfine-shifted ¹H resonances in oxidized and reduced putidaredoxin, an Fe₂S₂ ferredoxin from Pseudomonas putida. Magn. Reson. Chem. 31, S73-S77.
• Reipa, V., Holden, M.J., Mayhew, M.P. and Vilker, V.L. (2000) Temperature dependence of the formal reduction potential of putidaredoxin. Biochim. Biophys. Acta 1459, 1-9.
• 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.
• Sari, N., Holden, M.J., Mayhew, M.P., Vilker, V.L. and Coxon, B. (1998) Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues. Biochem. Biophys. Res. Commun. 249, 773-780.
• Sari, N., Holden, M.J., Mayhew, M.P., Vilker, V.L. and Coxon, B. (1999) Comparison of backbone dynamics of oxidized and reduced putidaredoxin by ¹⁵N NMR relaxation measurements. Biochemistry 38, 9862-9871. [Supplementary Material]
• Shimada, H., Nagano, S., Ariga, Y., Unno, M., Egawa, T., Hishiki, T., Ishimura, Y., Masuya, F., Obata, T. and Hori, H. (1999) Putidaredoxin-cytochrome P450_cam interaction. Spin state of the heme iron modulates putidaredoxin structure. J. Biol. Chem. 274, 9363-9369.
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• 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.
• Sugiura, Y., Ishizu, K. and Kimura, T. (1974) A rubredoxin-like mononuclear FeS₄ derivative of adrenal iron-sulfur protein (adrenodoxin). Biochem. Biophys. Res. Commun. 60, 334-340.
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• Takeuchi, K., Tsubaki, M., Futagawa, J., Masuyam F. and Hori, H. (2001) Adrenodoxin-cytochrome P450scc interaction as revealed by EPR spectroscopy: Comparison with the putidaredoxin-cytochrome P450cam system. J. Biochem. (Tokyo) 130, 789-797.
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• Weiss, R., Brachais, L., Lohr, F., Hartleib, J., Bernhardt, R. and Rüterjans, H. (2000) Assignment of ¹H, ¹³C and ¹⁵N signals of bovine adrenodoxin. J. Biomol. NMR 17, 355-356.
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Plant-type [Fe₂S₂] ferredoxins

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• 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.
• 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.
• 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.
• Canne, C., Ebelshäuser, M., Gay, E., Shergill, J.K., Cammack, R., Kappl, R. and Hüttermann, J. (2000) Probing magnetic properties of the reduced [2Fe-2S] cluster of the ferredoxin from Arthrospira platensis by ¹H ENDOR spectroscopy. J. Biol. Inorg. Chem. 5, 514-526.
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• 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.
• 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.
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• 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 2,3-dioxygenase. J. Biol. Chem. 273, 9622-9629.
• Hugo, N., Meyer, C., Armengaud, J., Gaillard, J., Timmis, K.N. and Jouanneau, Y. (2000) Characterization of three xylT-like [2Fe-2S] ferredoxins associated with catabolism of cresols or naphthalene: Evidence for their involvement in catechol dioxygenase reactivation. J. Bacteriol. 182, 5580-5585.
• Hurley, J.K., Caffrey, M.S., Markley, J.L., Cheng, H., Xia, B., Chae, Y.K., Holden, H.M. and Tollin, G. (1995) Mutations of surface residues in Anabaena vegetative and heterocyst ferredoxin that affect thermodynamic stability as determined by guanidine hydrochloride denaturation. Protein Science 4, 58-64.
• Hurley, J.K., Weber-Main, 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., Martinez-Júlvez, M., Gómez-Moreno, C., Schmeits, J.L. and Tollin, G. (1997a) Structure-function relationships in Anabaena ferredoxin: Correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP⁺ reductase for site-specific ferredoxin mutants. Biochemistry 36, 11100-11117.
• Hurley, J.K., Weber-Main, A.M., Hodges, A.E., Stankovich, M.T., Benning, M.M., Holden, H.M., Cheng, H., Xia, B., Markley, J.L., Genzor, C., Gómez-Moreno, C., Hafezi, R. and Tollin, G. (1997b) Iron-sulfur cluster cysteine-to-serine mutants of Anabaena [2Fe-2S] ferredoxin exhibit unexpected redox properties and are competent in electron transfer to ferredoxin:NADP⁺ reductase. Biochemistry 36, 15109-15117.
• Hurley, J.K., Faro, M., Brodie, T.B., Hazzard, J.T., Medina, M., Gómez-Moreno, C. and Tollin, G. (2000) Highly nonproductive complexes with Anabaena ferredoxin at low ionic strength are induced by nonconservative amino acid substitutions at Glu139 in Anabaena ferredoxin:NADP⁺ reductase. Biochemistry 39, 13695-13702.
• 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.
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