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Abstract:

Thermal perturbation of the dicluster ferredoxin from Acidianus ambivalens was investigated employing a toolbox of spectroscopic methods. FTIR and visible CD were used for assessing changes of the secondary structure and coarse alterations of the [3Fe4S] and [4Fe4S] cluster moieties, respectively. Fine details of the disassembly of the metal centers were revealed by paramagnetic NMR and resonance Raman spectroscopy. Overall, thermally induced unfolding of AaFd is initiated with the loss of α-helical content at relatively low temperatures (Tm app ∼ 44°C), followed by the disruption of both iron-sulfur clusters (Tm app sim; 53-60°C). The degradation of the metal centers triggers major structural changes on the protein matrix, including the loss of tertiary contacts (T m app ∼ 58°C) and a change, rather than a significant net loss, of secondary structure (Tm app ∼ 60°C). This latter process triggers a secondary structure reorganization that is consistent with the formation of a molten globule state. The combined spectroscopic approach here reported illustrates how changes in the metalloprotein organization are intertwined with disassembly of the iron-sulfur centers, denoting the conformational interplay of the protein backbone with cofactors. © 2007 American Chemical Society.

Registro:

Documento: Artículo
Título:A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties
Autor:Todorovic, S.; Leal, S.S.; Salgueiro, C.A.; Zebger, I.; Hildebrandt, P.; Murgida, D.H.; Gomes, C.M.
Filiación:Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av República EAN, 2781-901 Oeiras, Portugal
Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Quinta da Torre, 2825-114 Caparica, Portugal
Max-Volmer-Laboratorium für Biophysikalische Chemie, Institut für Chemie, Sekr. PC14, Strasse des 17 Juni 135, D-10623 Berlin, Germany
INQUIMAE-CONICET, Facultad de Ciencias Exactas Y Naturales, Pab.2, C1428EHA-Buenos Aires, Argentina
Palabras clave:Cofactors; Metalloproteins; Secondary structure; Thermal perturbation; Chemical modification; Conformations; Iron; Perturbation techniques; Raman spectroscopy; Sulfur; Proteins; ferredoxin; iron; sulfur; Acidianus; Acidianus ambivalens; alpha helix; article; conformational transition; electron spin resonance; infrared spectroscopy; low temperature; nonhuman; priority journal; protein conformation; protein folding; protein secondary structure; Raman spectrometry; structure analysis; temperature sensitivity; Acidianus; Circular Dichroism; Cysteine; Ferredoxins; Iron-Sulfur Proteins; Ligands; Magnetic Resonance Spectroscopy; Models, Molecular; Protein Folding; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Temperature; Transition Temperature; Acidianus ambivalens
Año:2007
Volumen:46
Número:37
Página de inicio:10733
Página de fin:10738
DOI: http://dx.doi.org/10.1021/bi700967g
Título revista:Biochemistry
Título revista abreviado:Biochemistry
ISSN:00062960
CODEN:BICHA
CAS:ferredoxin, 9040-09-9; iron, 14093-02-8, 53858-86-9, 7439-89-6; sulfur, 13981-57-2, 7704-34-9; Cysteine, 52-90-4; Ferredoxins; Iron-Sulfur Proteins; Ligands
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00062960_v46_n37_p10733_Todorovic

Referencias:

  • Wittung-Stafshede, P., Gomes, C.M., Teixeira, M., Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens (2000) J. Inorg. Biochem, 78, pp. 35-41
  • Leal, S.S., Teixeira, M., Gomes, C.M., Studies on the degradation pathway of iron-sulfur centers during unfolding of a hyperstable ferredoxin: Cluster dissociation, iron release and protein stability (2004) J. Biol. Inorg. Chem, 9, pp. 987-996
  • Leal, S.S., Gomes, C.M., Linear three-iron centres are unlikely cluster degradation intermediates during unfolding of iron-sulfur proteins (2005) Biol. Chem, 386, pp. 1295-1300
  • Fujii, T., Hata, Y., Oozeki, M., Moriyama, H., Wakagi, T., Tanaka, N., Oshima, T., The crystal structure of zinc-containing ferredoxin from the thermoacidophilic archaeon Sulfolobus sp. strain 7 (1997) Biochemistry, 36, pp. 1505-1513
  • Gomes, C., Faria, A., Carita, J., Mendes, J., Regalla, M., Chicau, P., Huber, H., Teixeira, M., Di-cluster, seven-iron ferredoxins from hyperthermophilic Sulfolobales (1998) J. Biol. Inorg. Chem, 3, pp. 499-507
  • Kojoh, K., Matsuzawa, H., Wakagi, T., Zinc and an N-terminal extra stretch of the ferredoxin from a thermoacidophilic archaeon stabilize the molecule at high temperature (1999) Eur. J. Biochem, 264, pp. 85-91
  • Rocha, R., Leal, S.S., Teixeira, V.H., Regalia, M., Huber, H., Baptista, A.M., Soares, C.M., Gomes, C.M., Natural domain design: Enhanced thermal stability of a zinc-lacking ferredoxin isoform shows that a hydrophobic core efficiently replaces the structural metal site (2006) Biochemistry, 45, pp. 10376-10384
  • Leal, S., Gomes, C.M., Studies of the molten globule state of ferredoxin: Structural characterisation and implications on protein folding and iron-sulfur centre assembly (2007) Proteins, 68 (3), pp. 606-616
  • Teixeira, M., Batista, R., Campos, A.P., Gomes, C., Mendes, J., Pacheco, I., Anemuller, S., Hagen, W.R., A seven-iron ferredoxin from the thermoacidophilic archaeon Desulfurolobus ambivalens (1995) Eur. J. Biochem, 227, pp. 322-327
  • Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F., Gilmanshin, R.I., Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe (1991) Biopolymers, 31, pp. 119-128
  • Bentrop, D., Bertini, I., Luchinat, C., Mendes, J., Piccioli, M., Teixeira, M., Paramagnetic NMR analysis of the seven-iron ferredoxin from the hyperthermoacidophilic archaeon Desulfurolobus ambivalens reveals structural similarity to other dicluster ferredoxins (1996) Eur. J. Biochem, 236, pp. 92-99
  • Czernuszewicz, R.S., Macor, K.A., Johnson, M.K., Gewirth, A., Spiro, T.G., Vibrational-Mode Structure and Symmetry in Proteins and Analogs Containing Fe4S4 Clusters - Resonance Raman Evidence for Different Degrees of Distortion in Hipip and Ferredoxin (1987) J. Am. Chem. Soc, 109, pp. 7178-7187
  • Duin, E.C., Lafferty, M.E., Crouse, B.R., Allen, R.M., Sanyal, I., Flint, D.H., Johnson, M.K., 2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthase (1997) Biochemistry, 36, pp. 11811-11820
  • Han, S., Czernuszewicz, R.S., Kimura, T., Adams, M.W.W., Spiro, T.G., Fe2S2 Protein Resonance Raman-Spectra Revisited - Structural Variations among Adrenodoxin, Ferredoxin, and Red Paramagnetic Protein (1989) J. Am. Chem. Soc, 111, pp. 3505-3511
  • Iwasaki, T., Watanabe, E., Ohmori, D., Imai, T., Urushiyama, A., Akiyama, M., Hayashi-Iwasaki, Y., Scott, R.A., Spectroscopic investigation of selective cluster conversion of archaeal zinc-containing ferredoxin from Sulfolobus sp strain 7 (2000) J. Biol. Chem, 275, pp. 25391-25401
  • Johnson, M. K., Czernuszewicz, R. S., Spiro, T. G., Fee, J. A., and Sweeney, W. V. (1983) Resonance Raman-Spectroscopic Evidence for a Common [3Fe-4S] Structure among Proteins Containing 3-Iron Centers, J. Am. Chem. Soc. 105, 6671-6678; Glasoe, P.K., Long, F.A., Use of Glass Electrodes to Measure Acidities in Deuterium Oxide (1960) J. Phys. Chem, 64, pp. 188-190
  • Arrondo, J.L., Muga, A., Castresana, J., Goni, F.M., Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy (1993) Prog. Biophys. Mol. Biol, 59, pp. 23-56
  • Byler, D.M., Susi, H., Examination of the secondary structure of proteins by deconvolved FTIR spectra (1986) Biopolymers, 25, pp. 469-487
  • Dong, A., Kendrick, B., Kreilgard, L., Matsuura, J., Manning, M.C., Carpenter, J.F., Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution (1997) Arch. Biochem. Biophys, 347, pp. 213-220
  • Jackson, M., Mantsch, H.H., The use and misuse of FTIR spectroscopy in the determination of protein structure (1995) Crit. Rev. Biochem. Mol. Biol, 30, pp. 95-120
  • Kunihiro, K., Arai, M., The molten globule state: The physical picture and biological significance (2000) Mechanisms of Protein Folding, , Pain, R. H, Ed, Oxford University Press: Oxford
  • Stephens, P.J., Jensen, G.M., Devlin, F.J., Morgan, T.V., Stout, C.D., Martin, A.E., Burgess, B.K., Circular dichroism and magnetic circular dichroism of Azotobacter vinelandii ferredoxin I (1991) Biochemistry, 30, pp. 3200-3209
  • Stephens, P. J., Thomson, A. J., Dunn, J. B., Keiderling, T. A., 7 Rawlings, J., Rao, K. K., and Hall, D. O. (1978) Circular dichroism and magnetic circular dichroism of iron-sulfur proteins, Biochemistry 17, 4770-4778; Lutz, M., Moulis, J.M., Meyer, J., Resonance Raman-Spectroscopy of Azotobacter-Vinelandii Ferredoxin. 1. Vibrational Features of the [3Fe-3S] Cluster (1983) FEBS Lett, 163, pp. 212-216

Citas:

---------- APA ----------
Todorovic, S., Leal, S.S., Salgueiro, C.A., Zebger, I., Hildebrandt, P., Murgida, D.H. & Gomes, C.M. (2007) . A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties. Biochemistry, 46(37), 10733-10738.
http://dx.doi.org/10.1021/bi700967g
---------- CHICAGO ----------
Todorovic, S., Leal, S.S., Salgueiro, C.A., Zebger, I., Hildebrandt, P., Murgida, D.H., et al. "A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties" . Biochemistry 46, no. 37 (2007) : 10733-10738.
http://dx.doi.org/10.1021/bi700967g
---------- MLA ----------
Todorovic, S., Leal, S.S., Salgueiro, C.A., Zebger, I., Hildebrandt, P., Murgida, D.H., et al. "A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties" . Biochemistry, vol. 46, no. 37, 2007, pp. 10733-10738.
http://dx.doi.org/10.1021/bi700967g
---------- VANCOUVER ----------
Todorovic, S., Leal, S.S., Salgueiro, C.A., Zebger, I., Hildebrandt, P., Murgida, D.H., et al. A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties. Biochemistry. 2007;46(37):10733-10738.
http://dx.doi.org/10.1021/bi700967g