A spectroscopic study of the temperature induced modifications on ferredoxin folding and iron-sulfur moieties

Biochemistry

Volumn 46, Issue 37, 2007, Pages 10733-10738

  Todorovic, Smilja ^a   Leal, Sónia S ^a   Salgueiro, Carlos A ^b   Zebger, Ingo ^c   Hildebrandt, Peter ^a,c   Murgida, Daniel H ^a,d   Gomes, Claúdio M ^a  

^a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^b UNIVERSIDADE NOVA DE LISBOA   (Portugal)

^c Sekr KWT 9   (Germany)

^d UNIVERSIDAD DE BUENOS AIRES   (Argentina)

Author keywords

[No Author keywords available]

Indexed keywords

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;

EID: 34548694529     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700967g     Document Type: Article

References (25)

1. Wittung-Stafshede, P., Gomes, C. M., and Teixeira, M. (2000) Stability and folding of the ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens, J. Inorg. Biochem. 78, 35-41.
2. Leal, S. S., Teixeira, M., and Gomes, C. M. (2004) Studies on the degradation pathway of iron-sulfur centers during unfolding of a hyperstable ferredoxin: cluster dissociation, iron release and protein stability, J. Biol. Inorg. Chem. 9, 987-996.
3. Leal, S. S., and Gomes, C. M. (2005) Linear three-iron centres are unlikely cluster degradation intermediates during unfolding of iron-sulfur proteins, Biol. Chem. 386, 1295-1300.
4. 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.
5. Gomes, C., Faria, A., Carita, J., Mendes, J., Regalla, M., Chicau, P., Huber, H., Stetter, K., and Teixeira, M. (1998) Di-cluster, seven-iron ferredoxins from hyperthermophilic Sulfolobales, J. Biol. Inorg. Chem. 3, 499-507.
6. 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.
7. Rocha, R., Leal, S. S., Teixeira, V. H., Regalia, M., Huber, H., Baptista, A. M., Soares, C. M., and Gomes, C. M. (2006) Natural domain design: enhanced thermal stability of a zinc-lacking ferredoxin isoform shows that a hydrophobic core efficiently replaces the structural metal site, Biochemistry 45, 10376-10384.
8. Leal, S., and Gomes, C. M. (2007) Studies of the molten globule state of ferredoxin: structural characterisation and implications on protein folding and iron-sulfur centre assembly, Proteins 68(3), 606-616.
9. Teixeira, M., Batista, R., Campos, A. P., Gomes, C., Mendes, J., Pacheco, I., Anemuller, S., and Hagen, W. R. (1995) A seven-iron ferredoxin from the thermoacidophilic archaeon Desulfurolobus ambivalens, Eur. J. Biochem. 227, 322-327.
10. Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., and Gilmanshin, R. I. (1991) Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe, Biopolymers 31, 119-128.
11. 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.
12. Czernuszewicz, R. S., Macor, K. A., Johnson, M. K., Gewirth, A., and Spiro, T. G. (1987) Vibrational-Mode Structure and Symmetry in Proteins and Analogs Containing Fe4S4 Clusters - Resonance Raman Evidence for Different Degrees of Distortion in Hipip and Ferredoxin, J. Am. Chem. Soc. 109, 7178-7187.
13. Duin, E. C., Lafferty, M. E., Crouse, B. R., Allen, R. M., Sanyal, I., Flint, D. H., and Johnson, M. K. (1997) [2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthase, Biochemistry 36, 11811-11820.
14. Han, S., Czernuszewicz, R. S., Kimura, T., Adams, M. W. W., and Spiro, T. G. (1989) Fe2S2 Protein Resonance Raman-Spectra Revisited - Structural Variations among Adrenodoxin, Ferredoxin, and Red Paramagnetic Protein, J. Am. Chem. Soc. 111, 3505-3511.
15. Iwasaki, T., Watanabe, E., Ohmori, D., Imai, T., Urushiyama, A., Akiyama, M., Hayashi-Iwasaki, Y., Cosper, N. J., and Scott, R. A. (2000) Spectroscopic investigation of selective cluster conversion of archaeal zinc-containing ferredoxin from Sulfolobus sp strain 7, J. Biol. Chem. 275, 25391-25401.
16. 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.
17. Glasoe, P. K., and Long, F. A. (1960) Use of Glass Electrodes to Measure Acidities in Deuterium Oxide, J. Phys. Chem. 64, 188-190.
18. Arrondo, J. L., Muga, A., Castresana, J., and Goni, F. M. (1993) Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy, Prog. Biophys. Mol. Biol. 59, 23-56.
19. Byler, D. M., and Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra, Biopolymers 25, 469-487.
20. Dong, A., Kendrick, B., Kreilgard, L., Matsuura, J., Manning, M. C., and Carpenter, J. F. (1997) Spectroscopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution, Arch. Biochem. Biophys. 347, 213-220.
21. Jackson, M., and Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure, Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
22. Kunihiro, K., and Arai, M. (2000) The molten globule state: the physical picture and biological significance, in Mechanisms of Protein Folding (Pain, R. H., Ed.) Oxford University Press: Oxford.
23. 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.
24. 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.
25. Lutz, M., Moulis, J. M., and Meyer, J. (1983) Resonance Raman-Spectroscopy of Azotobacter-Vinelandii Ferredoxin. 1. Vibrational Features of the [3Fe-3S] Cluster, FEBS Lett. 163, 212-216.