Structural studies of high-potential iron proteins (HiPIP)

Last modified: Wed Apr 14 12:14:42 BST 2004

• Adman, E.T., Mather, M.W. and Fee, J.A. (1993) Molecular modeling studies on the proposed NaCl-induced dimerization of Chromatium vinosum high-potential iron protein. Biochim. Biophys. Acta 1142, 93-98.
• Agarwal, A., Li, D. and Cowan, J.A. (1995) Role of aromatic residues in stabilization of the [Fe₄S₄] cluster in high-potential iron proteins (HiPIPs): Physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP. Proc. Natl. Acad. Sci. USA 92, 9440-9444.
• Agarwal, A., Li, D. and Cowan, J.A. (1996) Influence of oxygen ligation on [Fe₄S₄] cluster properties. Characterization of the Cys77Ser mutant of Chromatium vinosum HiPIP. J. Am. Chem. Soc. 118, 927-928.
• Anderson, R.E., Anger, G., Petersson, L., Ehrenberg, A., Cammack, R., Hall, D.O., Mullinger, R. and Rao, K.K. (1975) The iron electron-nuclear double resonance (ENDOR) of 4-Fe clusters in iron-sulfur proteins from Chromatium and Clostridium pasteurianum. Biochim. Biophys. Acta 376, 63-71.
• Babini, E., Bertini, I., Borsari, M., Capozzi, F., Dikiy, A., Eltis, L.D. and Luchinat, C. (1996) A cysteine  serine ligand mutation in the high potential iron-sulfur protein from Chromatium vinosum provides insight into the electronic structure of the [4Fe-4S] cluster. J. Am. Chem. Soc. 118, 75-80.
• Babini, E., Borsari, M., Capozzi, F., Eltis, L.D. and Luchinat, C. (1999) Experimental evidence for the role of buried polar groups in determining the reduction potential of metalloproteins: the S79P variant of Chromatium vinosum HiPIP. J. Biol. Inorg. Chem. 4, 692-700.
• Babini, E., Bertini, I., Borsari, M., Capozzi, F., Luchinat, C., Zhang, X., Moura, G.L.C., Kurnikov, I.V., Beratan, D.N., Ponce, A., Di Bilio, A.J., Winkler, J.R. and Gray, H.B. (2000) Bond-mediated electron tunneling in ruthenium-modified high-potential iron-sulfur protein. J. Am. Chem. Soc. 122, 4532-4533. [Supplementary Material]
• Banci, L., Bertini, I., Ciurli, S., Ferretti, S., Luchinat, C. and Piccioli, M. (1993) The electronic structure of [Fe₄S₄]³⁺ clusters in proteins. An investigation of the oxidized high-potential iron-sulfur protein II from Ectothiorhodospira vacuolata. Biochemistry 32, 9387-9397.
• Banci, L., Bertini, I., Eltis, L.D., Felli, I.C., Kastrau, D.H.W., Luchinat, C., Piccioli, M., Pierattelli, R. and Smith, M. (1994) The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonance. Eur. J. Biochem. 225, 715-725.
• Banci, L., Bertini, I., Dikiy, A., Kastrau, D.H.W., Luchinat, C. and Sompornpisut, P. (1995) The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR. Biochemistry 34, 206-219.
• Benning, M.M., Meyer, T.E., Rayment, I. and Holden, H.M. (1994) Molecular structure of the oxidized high-potential iron-sulfur protein isolated from Ectothiorhodospira vacuolata. Biochemistry 33, 2476-2483.
• Bentrop, D., Bertini, I., Capozzi, F., Dikiy, A., Eltis, L. and Luchinat, C. (1996) Three-dimensional structure of the reduced C77S mutant of the Chromatium vinosum high-potential iron-sulfur protein through nuclear magnetic resonance: Comparison with the solution structure of the wild-type protein. Biochemistry 35, 5928-5936.
• Bentrop, D., Bertini, I., Iacoviello, R., Luchinat, C., Niikura, Y., Piccioli, M., Presenti, C. and Rosato, A. (1999) Structural and dynamical properties of a partially unfolded Fe₄S₄ protein: Role of the cofactor in protein folding. Biochemistry 38, 4669-4680. [Supplementary Material]
• Bertini, I., Capozzi, F., Luchinat, C. and Piccioli, M. (1993a) ¹H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis. Eur. J. Biochem. 212, 69-78.
• Bertini, I., Gaudemer, A., Luchinat, C. and Piccioli, M. (1993b) Electron self-exchange in high-potential iron-sulfur proteins. Characterization of protein I from Ectothiorhodospira vacuolata. Biochemistry 32, 12887-12893.
• Bertini, I., Felli, I.C., Kastrau, D.H.W., Luchinat, C., Piccioli, M. and Viezzoli, M.S. (1994) Sequence-specific assignment of the ¹H and ¹⁵N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila. Eur. J. Biochem. 225, 703-714.
• Bertini, I., Dikiy, A., Kastrau, D.H.W., Luchinat, C. and Sompornpisut, P. (1995) Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species. Biochemistry 34, 9851-9858.
• Bertini, I., Felli, I.C., Luchinat, C. and Rosato, A. (1996a) A complete relaxation matrix refinement of the solution structure of a paramagnetic metalloprotein: Reduced HiPIP I from Ectothiorhodospira halophila. Proteins 24, 158-164.
• Bertini, I., Couture, M.M.J., Donaire, A., Eltis, L.D., Felli, I.C., Luchinat, C., Piccioli, M. and Rosato, A. (1996b) The solution structure refinement of the paramagnetic reduced high-potential iron-sulfur protein I from Ectothiorhodospira halophila by using stable isotope labeling and nuclear relaxation. Eur. J. Biochem. 241, 440-452.
• Bertini, I., Borsari, M., Bosi, M., Eltis, L.D., Felli, I.C., Luchinat, C. and Piccioli, M. (1996c) The influence of a surface charge on the electronic and steric structure of a high potential iron-sulfur protein. J. Biol. Inorg. Chem. 1, 257-263.
• Bertini, I., Donaire, A., Felli, I.C., Luchinat, C. and Rosato, A. (1997a) ¹H and ¹³C NMR studies of an oxidized HiPIP. Inorg. Chem. 36, 4798-4803.
• Bertini, I., Cowan, J.A., Luchinat, C., Natarajan, K. and Piccioli, M. (1997b) Characterization of a partially unfolded high potential iron protein. Biochemistry 36, 9332-9339.
• 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.
• Bian, S. and Cowan, J.A. (1998) Biological iron-sulfur cluster assembly. Detection of kinetic intermediates by time-resolved fluorescence spectroscopy. J. Am. Chem. Soc. 120, 3532-3533.
• Bian, S., Hemann, C.F., Hille, R. and Cowan, J.A. (1996) Characterization of an autoreduction pathway for the [Fe₄S₄]³⁺ cluster of mutant Chromatium vinosum high-potential iron proteins. Site-directed mutagenesis studies to probe the role of phenylalanine 66 in defining the stability of the [Fe₄S₄] center provide evidence for oxidative degradation via a [Fe₃S₄] cluster. Biochemistry 35, 14544-14552.
• Breiter, D.R., Meyer, T.E., Rayment, I. and Holden, H.M. (1991) The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-Å resolution. J. Biol. Chem. 266, 18660-18667.
• Carter, C.W., Jr., Kraut, J., Freer, S.T., Xuong, Ng.-H., Alden, R.A. and Bartsch, R.G. (1974) 2-Å crystal structure of oxidized Chromatium high potential iron protein. J. Biol. Chem. 249, 4212-4225.
• Ciszewska, H., Bagyinka, C., Tigyi, G. and Kovacs, K.L. (1989) Purification and properties of high potential iron-sulphur protein from Thiocapsa roseopersicina. Acta Biochim. Biophys. Hung. 24, 361-375.
• Ciurli, S., Cremonini, M.A., Kofod, P. and Luchinat, C. (1996) ¹H NMR of high-potential iron-sulfur protein from the purple non-sulfur bacterium Rhodoferax fermentans. Eur. J. Biochem. 236, 405-411.
• Couture, M.M.J., Auger, M., Rosell, F., Mauk, A.G., Boubour, E., Lennox, R.B. and Eltis, L.D. (1999) Investigation of the role of a surface patch in the self-association of Chromatium vinosum high potential iron-sulfur protein. Biochim. Biophys. Acta 1433, 159-169.
• Cowan, J.A. and Sola, M. (1990) ¹H NMR studies of oxidized high-potential iron protein from Chromatium vinosum. Nuclear Overhauser effect measurements. Biochemistry 29, 5633-5637.
• Dilg, A.W.E., Mincione, G., Achterhold, K., Iakovleva, O., Mentler, M., Luchinat, C., Bertini, I. and Parak, F.G. (1999) Simultaneous interpretation of Mössbauer, EPR and ⁵⁷Fe ENDOR spectra of the [Fe₄S₄] cluster in the high-potential iron protein I Ectothiorhodospira halophila. J. Biol. Inorg. Chem. 4, 727-741.
• Dilg, A.W.E., Capozzi, F., Mentler, M., Iakovleva, O., Luchinat, C., Bertini, I. and Parak, F.G. (2001) Comparison and characterization of the [Fe₄S₄]^2+/3+ centre in the wild-type and C77S mutated HiPIPs from Chromatium vinosum monitored by Mössbauer, ⁵⁷Fe ENDOR and EPR spectroscopies. J. Biol. Inorg. Chem. 6, 232-246.
• Dunham, W.R., Hagen, W.R., Fee, J.A., Sands, R.H., Dunbar, J.B. and Humblet, C. (1991) An investigation of Chromatium vinosum high-potential iron-sulfur protein by EPR and Mössbauer spectroscopy; evidence for a freezing-induced dimerization in NaCl solutions. Biochim. Biophys. Acta 1079, 253-262.
• Foster, M.W., Bian, S., Surerus, K.K. and Cowan, J.A. (2001) Elucidation of a [4Fe-4S] cluster degradation pathway: rapid kinetic studies of the degradation of Chromatium vinosum HiPIP. J. Biol. Inorg. Chem. 6, 266-274.
• Freer, S.T., Alden, R.A., Carter, C.W., Jr. and Kraut, J. (1975) Crystallographic structure refinement of Chromatium high potential iron protein at 2 Å resolution. J. Biol. Chem. 250, 46-54.
• Gaillard, J., Albrand, J.-P., Moulis, J.-M. and Wemmer, D.E. (1992) Sequence-specific assignments of the ¹H nuclear magnetic resonance spectra of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum. Biochemistry 31, 5632-5639.
• Heering, H.A., Bulsink, Y.B.M., Hagen, W.R. and Meyer, T.E. (1995) Reversible super-reduction of the cubane [4Fe-4S]^(3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions. EPR spectroscopic and electrochemical studies. Eur. J. Biochem. 232, 811-817.
• Hochkoeppler, A., Kofod, P., Ferro, G. and Ciurli, S. (1995) Isolation, characterization, and functional role of the high-potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans. Arch. Biochem. Biophys. 322, 313-318.
• Holden, H.M., Meyer, T.E., Cusanovich, M.A. and Rayment, I. (1986) Crystallization of a high potential iron-sulfur protein from the halophilic phototrophic bacterium Ectothiorhodospira halophila. J. Biol. Chem. 261, 14746-14747.
• Huber, J.G., Moulis, J.-M. and Gaillard, J. (1996) Use of ¹H longitudinal relaxation times in the solution structure of paramagnetic proteins. Application to [4Fe-4S] proteins. Biochemistry 35, 12705-12711.
• Iwagami, S.G., Creagh, A.L., Haynes, C.A., Borsari, M., Felli, I.C., Piccioli, M. and Eltis, L.D. (1995) The role of a conserved tyrosine residue in high-potential iron sulfur proteins. Protein Science 4, 2562-2572.
• Johnson, M.K., Thomson, A.J., Robinson, A.E., Rao, K.K. and Hall, D.O. (1981) Low-temperature magnetic circular dichroism spectra and magnetisation curves of 4Fe clusters in iron-sulphur proteins from Chromatium and Clostridium pasteurianum. Biochim. Biophys. Acta 667, 433-451.
• Kappl, R., Ciurli, S., Luchinat, C. and Hüttermann, J. (1999) Probing structural and electronic properties of the oxidized [Fe₄S₄]³⁺ cluster of Ectothiorhodospira halophila iso-II high-potential iron-sulfur protein by ENDOR spectroscopy. J. Am. Chem. Soc. 121, 1925-1935.
• Kerfeld, C.A., Salmeen, A.E. and Yeates, T.O. (1998) Crystal structure and possible dimerization of the high-potential iron-sulfur protein from Chromatium purpuratum. Biochemistry 37, 13911-13917.
• Krishnamoorthi, R., Markley, J.L., Cusanovich, M.A., Przysiecki, C.T. and Meyer, T.E. (1986) Hydrogen-1 nuclear magnetic resonance investigation of high-potential iron-sulfur proteins from Ectothiorhodospira halophila and Ectothiorhodospira vacuolata: A comparative study of hyperfine-shifted resonances. Biochemistry 25, 60-67.
• Krishnamoorthi, R., Cusanovich, M.A., Meyer, T.E. and Przysiecki, C.T. (1989) ¹H-NMR studies of high-potential iron-sulfur protein from the purple phototrophic bacterium, Rhodospirillum tenue. Eur. J. Biochem. 181, 81-85.
• Li, D., Cottrell, C.E. and Cowan, J.A. (1995) ¹⁵N resonance assignments of oxidized and reduced Chromatium vinosum high-potential iron protein. J. Protein Chem. 14, 115-126.
• Natarajan, K. and Cowan, J.A. (1997) Identification of a key intermediate of relevance to iron-sulfur cluster biosynthesis. Mechanism of cluster assembly and implications for protein folding. J. Am. Chem. Soc. 119, 4082-4083.
• Nettesheim, D.G., Harder, S.R., Feinberg, B.A. and Otvos, J.D. (1992) Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosum. Biochemistry 31, 1234-1244.
• Nogi, T., Kobayashi, M., Nozawa, T. and Miki, K. (2000) Crystallization and preliminary crystallographic analysis of the high-potential iron-sulfur protein from Thermochromatium tepidum. Acta Crystallogr. D56, 656-658.
• Parisini, E., Capozzi, F., Lubini, P., Lamzin, V., Luchinat, C. and Sheldrick, G.M. (1999) Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution. Acta Crystallogr. D55, 1773-1784.
• Peisach, J., Orme-Johnson, N.R., Mims, W.B. and Orme-Johnson, W.H. (1977) Linear electric field effect and nuclear modulation studies of ferredoxins and high potential iron-sulfur proteins. J. Biol. Chem. 252, 5643-5650.
• Pereira, M.M., Antunes, A.M., Nunes, O.C., da Costa, M.S. and Teixeira, M. (1994) A membrane-bound HIPIP-type center in the thermohalophile Rhodothermus marinus. FEBS Lett. 352, 327-330.
• Pereira, M.M., Carita, J.N. and Teixeira, M. (1999a) Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: characterization of the iron-sulfur centers from the dehydrogenases and investigation of the high-potential iron-sulfur protein function by in vitro reconstitution of the respiratory chain. Biochemistry 38, 1276-1283.
• Pereira, M.M., Santana, M., Soares, C.M., Mendes, J., Carita, J.N., Fernandes, A.S., Saraste, M., Carrondo, M.A. and Teixeira, M. (1999b) The caa₃ terminal oxidase of the thermohalophilic bacterium Rhodothermus marinus: a HiPIP:oxygen oxidoreductase lacking the key glutamate of the D-channel. Biochim. Biophys. Acta 1413, 1-13.
• Phillips, W.D., Poe, M., McDonald, C.C. and Bartsch, R.G. (1970) Proton magnetic resonance studies of Chromatium high-potential iron protein. Proc. Natl. Acad. Sci. USA 67, 682-687.
• Przysiecki, C.T., Meyer, T.E. and Cusanovich, M.A. (1985) Circular dichroism and redox properties of high redox potential ferredoxins. Biochemistry 24, 2542-2549.
• Rayment, I., Wesenberg, G., Meyer, T.E., Cusanovich, M.A. and Holden, H.M. (1992) Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 Å resolution. J. Mol. Biol. 228, 672-686.
• 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.
• Soriano, A., Li, D., Bian, S., Agarwal, A. and Cowan, J.A. (1996) Factors influencing redox thermodynamics and electron self-exchange for the [Fe₄S₄] cluster in Chromatium vinosum high potential iron protein: The role of core aromatic residues in defining cluster redox chemistry. Biochemistry 35, 12479-12486.
• Stephens, P.J., Thomson, A.J., Keiderling, T.A., Rawlings, J., Rao, K.K. and Hall, D.O. (1978a) Cluster characterization in iron-sulfur proteins by magnetic circular dichroism. Proc. Natl. Acad. Sci. USA 75, 5273-5275.
• Stephens, P.J., Thomson, A.J., Dunn, J.B., Keiderling, T.A., Rawlings, J., Rao, K.K. and Hall, D.O. (1978b) Circular dichroism and magnetic circular dichroism of iron-sulfur proteins. Biochemistry 17, 4770-4778.
• Szokefalvi-Nagy, Z., Bagyinka, C., Demeter, I., Kovacs, K.L. and Quynh, L.H. (1990) Location and quantification of metal ions in enzymes combining polyacrylamide gel electrophoresis and particle-induced X-ray emission. Biol. Trace Elem. Res. 26-27, 93-101.

Back to the Directory of P450-containing Systems home page:

Trieste site

Gödöllõ site