Reversible, non-denaturing metal substitution in bovine adrenodoxin and spinach ferredoxin and the different reactivities of [2Fe-2S]-cluster-containing proteins

European Journal of Biochemistry

Volumn 239, Issue 3, 1996, Pages 818-826

  Iametti, Stefania ^a   Uhlmann, Heike ^b   Sala, Nicla ^a   Bernhardt, Rita ^b   Ragg, Enzio ^a   Bonomi, Francesco ^a,c  

^a UNIVERSITY OF MILAN   (Italy)

^b SAARLAND UNIVERSITY   (Germany)

^c Dipto Sci Molecolari A   (Italy)

Author keywords

Adrenodoxin; Iron sulfur cluster; Metal substitution; Spinach ferredoxin

Indexed keywords

ADRENODOXIN; CADMIUM; FERREDOXIN; IRON SULFUR PROTEIN; METAL; ZINC;

ARTICLE; BLEACHING; CATTLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DRUG ACTIVITY; ELECTRON SPIN RESONANCE; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN MODIFICATION; SPECTROPHOTOMETRY; SPINACH;

BOS TAURUS; BOVINAE; SPINACIA OLERACEA;

EID: 0030015446     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0818u.x     Document Type: Article

References (46)

1. Moura, J. J. G., Macedo, A. L. & Palma, P. N. (1995) Ferredoxins, Methods Enzymol. 243, 165-188.
2. Emptage, M. H., Kent, T. A., Huynh, B. H., Rawlings, J., Orme-Johnson, W. H. & Münck, E. (1980) On the nature of the iron-sulfur centers in a ferredoxin from Azotobacter vinelandii. Mössbauer studies and cluster displacement experiments, J. Biol. Chem. 255, 1793-1796.
3. Antonio, M. R., Averill, B. A., Moura, I., Moura, J. J. G., Orme-Johnson, W. H., Teo, B. K. & Xavier, A. V. (1982) Core dimensions in the 3Fe cluster of Desulfovibrio gigas ferredoxin II by extended X-ray absorption fine structure spectroscopy, J. Biol. Chem. 257, 6646-6649.
4. Beinert, H. & Kennedy, M. C. (1989) Engineering of protein bound iron-sulfur clusters. A tool for the study of protein and cluster chemistry and mechanism of iron-sulfur enzymes, Eur. J. Biochem. 186, 5-15.
5. Rouault, T. A., Stout, C. D., Kaptain, S., Harford, J. B. & Klausner, R. D. (1991) Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: functional implications, Cell 64, 881-883.
6. Lauble, H., Kennedy, M. C., Beinert, H. & Stout, C. D. (1992) Crystal structures of aconitase with isocitrate and nitroisocitrate bound, Biochemistry 31, 2735-2748.
7. Thomson, A. J. (1991) Does ferredoxin I (Azotobacter) represent a novel class of DNA-binding proteins that regulate gene expression response to cellular iron (II)? FEBS Lett. 285, 230-236.
8. O'Halloran, T. V. (1993) Transition metals in control of gene expression, Science 261, 715-725.
9. 4 cluster in Pyrococcus furiosus ferredoxin, J. Am. Chem. Soc. 112, 4562-4564.
10. +1 centers in a ferredoxin, J. Am. Chem Soc. 113, 8948-8950.
11. 1 complex, Eur. J. Biochem. 197, 555-561.
12. Bonomi, F., Ganadu, M. L., Lubinu, G. & Pagani, S. (1994) Reversible, non-denaturing substitution of iron by cadmium in Clostridium pasteurianum ferredoxin, Eur. J. Biochem. 222, 639-644.
13. Arendsen, A. F., Schalk, J., Van Dongen, W. M. A. M. & Hagen, W. R. (1995) Characterization of a ferredoxin from Desulfovibrio vulgaris (Hildenborough) that interacts with RNA. Eur J. Biochem. 231, 352-357.
14. Sugiura, Y., Ishizu, K. & Kimura, T. (1975) Cobalt and ruthenium replacement for iron in adrenal iron-sulfur protein (adrenodoxin). Preparation and some properties, Biochemistry 14, 97-101.
15. 4 derivative of adrenal iron-sulfur protein (adrenodoxin), Biochem. Biophys. Res. Commun. 60, 334-340.
16. Hidalgo, E. & Demple, B. (1994) An iron-sulfur center essential for transcriptional activation by the redox-sensing SoxR protein, EMBO J. 13, 138-146.
17. Tomsett, A. B., Sewell, A. K., Jones, S. J., de Miranda, J. R. & Thurman, D. A. (1992) Metal-binding proteins and metal-regulated gene expression in higher plants, Soc. Exp. Biol. Semin. Ser. 49, 1-24.
18. Petering, D. H. & Palmer, G. (1970) Properties of spinach ferredoxin in aerobic urea solution: a comparison with the native protein, Arch. Biochem. Biophys. 141, 456-464.
19. Sakihama, N., Shin, M. & Toda, H. (1986) Separation and identification of two native forms of spinach ferredoxin by hydrophobic chromatography, J. Biochem. (Tokyo) 100, 43-47.
20. Uhlmann, H., Beckert, V., Schwarz, D. & Bernhardt, R. (1992) Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of 2Fe-2S cluster ligands, Biochem. Biophys. Res. Commun. 188, 1131-1138.
21. Huang, J. J. & Kimura, T. (1973) Adrenal steroid hydroxylases. Oxidation-reduction properties of adrenal iron-sulfur protein (adrenodoxin), Biochemistry 12, 406-409.
22. Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
23. Timcenko, L. & Kimura, T. (1979) Liberation of labile sulfur from ferredoxins by alkaline zinc reagent: an appraisal of the methylene blue method, Anal. Biochem. 95, 452-457.
24. Ljones, T. & Burris, R. H. (1978) Nitrogenase: the reaction between iron protein and bathophenanthrolinedisulfonate as a probe for interactions with MgATP, Biochemistry 17, 1866-1872.
25. Uhlmann, H., Kraft, R. & Bernhardt, R. (1994) C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450, J. Biol. Chem. 269, 22557-22564.
26. + oxidoreductase, Methods Enzymol. 69, 250-255.
27. 1H NMR studies on the oxidized ferredoxin from Clostridium pasteurianum, Biochem. Int. 26, 577-585.
28. 15N-NMR, Protein Sci. 4, 100.
29. Vašk, M. & Kägi, J. H. R. (1983)Spectroscopic properties of metallothionein, Metal Ions Biol. Syst. 15, 213-273.
30. Pagani, S., Vecchio, G., Iametti, S., Bianchi, R. & Bonomi, F. (1986) On the role of the 2Fe-2S cluster in the formation of the structure of spinach ferredoxin. Biochim. Biophys. Acta 870, 538-544.
31. 2 (n = 2,4) in aqueous media from iron salts, thiols, and sulfur, sulfide or thiosulfate plus rhodanese, Inorg. Chem. 24, 4431-4335.
32. May, S. W. & Kuo, J.-Y. (1978) Prepartion and properties of Cobalt (II) rubredoxin, Biochemistry 17, 3333-3338.
33. Bonomi, F., Pagani, S. & Kurtz, D. M. Jr (1985) Enzymic synthesis of the 4Fe-4S clusters of Clostridium pasteurianum ferredoxin, Eur. J. Biochem. 148, 67-73.
34. Pagani, S., Bonomi, F. & Cerletti, P. (1984) Enzymic synthesis of 8 the iron-sulfur cluster of spinach ferredoxin, Eur. J. Biochem. 142, 361-366.
35. Speiser, D. M., Abrahamson, S. L., Banuelos, G. & Ow, D. W. (1992) Brassica juncea produces a phytochelatin-cadmium-sulfide complex, Plant Physiol. (Bethesda) 99, 817-821.
36. Iametti, S., Sala, N., Uhlmann, H., Beckert, V., Bernhardt, R. & Bonomi, F. (1995) Substitution of cluster iron by zinc and cadmium in wild-type and mutated adrenodoxin, Abstr. Commun. 7th International Conference on Bio-Inorganic Chemistry, Lübeck, Germany.
37. Beckert, V., Schrauber, H., Bernhardt, R., van Dijk, A. A., Kakoschke, C. & Wray, V. (1995) Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications, Eur. J. Biochem. 231, 116-235.
38. Uhlmann, H. & Bernhardt, R. (1995) The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function, J. Biol. Chem. 270, 29959-29966.
39. Piubelli, L., Bellintani, F., Aliverti, A. & Zanetti, G. (1995) Heterologous synthesis in E. coli and characterization of wild-type and mutant forms of spinach ferredoxin I. Protein Sci. 4, 60.
40. Khoroshilova, N., Beinert, H. & Kiley, P. J. (1995) Association of a polynuclear iron-sulfur center with a mutant FNR protein enhances DNA binding, Proc. Natl. Acad. Sci. USA 92, 2499-2503.
41. Elliot, R. C., Dickey, L. F., White, M. J. & Thompson, W. F. (1989) Cis-acting elements for light regulation of pea ferredoxin I gene expression are located within transcribed sequences, Plant Cell 1, 691-698.
42. Tomsett, A. B. & Thurman, D. A. (1988) Molecular biology of metal tolerances in plants, Plant Cell Environ. 11, 383-394.
43. Jackson, P. J., Unkefer, P. J., Delhaize, E. & Robinson, N. J. (1990) Mechanisms of trace metal tolerance in plants, in Environmental injury in plants (Katterman. F., ed.), pp. 231-255, Academic Press, San Diego.
44. 2 during unstimulated steroid synthesis, Cell. Biol. Toxicol. 10, 23-33.
45. Colby, H. D. (1981) Chemical suppression of steroidogenesis, Environ. Health Perspect. 38, 119-127.
46. Warner, M. (1983) Evidence for a dioxygenase activity of solubilized renal mitochondrial cytochrome P-450. J. Biol. Chem. 258, 11590-11593.