Keywords: Copper Ion, Cysteine, Ferric Ion, Ferrous Ion, Iron Binding Protein, Iron Sulfur Protein, Metal Complex, Metal Ion, Metalloprotein, Miniaturized Electron Transfer Protein, Rubredoxin, Unclassified Drug, Zinc Ion, Amino Acid Sequence, Article, Circular Dichroism, Controlled Study, Desulfovibrio Vulgaris, Metal Binding, Methodology, Molecular Model, Nonhuman, Nuclear Magnetic Resonance, Priority Journal, Protein Synthesis, Stoichiometry, Structure Analysis, Ultraviolet Radiation, Iron-Sulfur Proteins, Miniaturization, Biomolecular, Protein Binding, Spectrophotometry, Bacteria (microorganisms),
Affiliations: Department of Chemistry, University of Napoli Federico II, Via Mezzocannone 4, I-80134 Napoli, Italy
Ctro. di Stud. di Biocristallografia, C.N.R., Via Mezzocannone 4, 1-80134 Napoli, Italy
Wuthrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley, New York
Pavone, V., (1988) Int. J. Biol. Macromol., 10, pp. 238-240
Pavone, V., Gaeta, G., Lombardi, A., Nastri, F., Maglio, O., Isernia, C., Saviano, M., (1996) Biopolymers, 38, pp. 705-721
Gunasekaran, K., Ramakrishnan, C., Balaram, P., (1997) Protein Eng., 10, pp. 1131-1141
Pavone, V., Di Blasio, B., Santini, A., Benedetti, E., Pedone, C., Toniolo, C., Crisma, M., (1990) J. Mol. Biol., 214, pp. 633-635
Bertini, I., Luchinat, C., (1984) Adv. Inorg. Biochim., 6, pp. 71-111
Fasman, G.D., (1996) Circular Dichroism and Conformationl Analysis of Biomolecules, , Plenum, New York
Cunningham, B. C., Wells, J. A., (1997) Curr. Opin. Struct. Biol., 7, pp. 457-46
DeGrado, W. F., Summa, C. M., Pavone, V., Nastri, F., Lombardi, A., (1999) Annu. Rev. Biochem., 68, pp. 779-819
Hellinga, H. W., (1998) Folding Des., 3, pp. R1-R8
Lippard, S. J., Berg, J. M., (1994) Principles of Bioinorganic Chemistry, pp. 349-378. , University Science Books, Mill Valley, CA
Choma, C. T., Lear, J. D., Nelson, M. J., Dutton, P. L., Robertson, D. E., DeGrado, W. F., (1994) J. Am. Chem. Soc., 116, pp. 856-865
Gibney, B. R., Mulholland, S. E., Rabanal, F., Dutton, P. L., (1996) Proc. Natl. Acad. Sci. USA, 93, pp. 15041-15046
Arnold, P. A., Shelton, W. R., Benson, D. R., (1997) J. Am. Chem. Soc., 119, pp. 3181-3182
Summa, C. M., Lombardi, A., Lewis, M., DeGrado, W. F., (1999) Curr. Opin. Struct. Biol., 9, pp. 500-508
Sieker, L. C., Stenkamp, R. E., Legall, J., (1994) Methods Enzymol., 243, pp. 203-216
Bau, R., Rees, D. C., Kurtz, D. M., Scott, J. A. R., (1998) J. Biol. Inorg. Chem., 3, pp. 484-493
Watenpaugh, K. D., Sieker, L. C., Jensen, L. H., (1980) J. Mol. Biol., 138, pp. 615-633
Im, S. -C., Sykes, A. G., (1996) J. Chem. Soc. Dalton Trans., pp. 2219-2222
Richie, K. A., Teng, Q., Elkin, C. J., Kurtz Jr., D. M., (1996) Protein Sci., 5, pp. 883-894
Blake, P. R., Park, J. -B., Zhou, Z. H., Hare, D. R., Adam, M. W., Summers, M. F., (1992) Protein Sci., 1, pp. 1508-1521
Maher, M. J., Xiao, Z., Wilce, M. C. J., Guss, M., Wedd, A. G., (1999) Acta Crystallogr. D, 55, pp. 962-968
Eidness, M. K., Burden, A. E., Richie, K. A., Kurtz, D. M., Scott, R. A., Smith, E. T., Ichiye, T., Kang, C., (1999) Biochemistry, 38, pp. 14803-14809
May, S. W., Kuo, J. Y., (1978) Biochemistry, 17, pp. 3333-3338
Christensen, H. E. M., Hammerstad-Pedersen, J. M., Holm, A., Roepstorff, P., Ulstrup, J., Vorm, O., Ostergard, S., (1992) FEBS Lett., 312, pp. 219-222
Anglin, J. R., Davison, A., (1975) Inorg. Chem., 14, pp. 234-237
Lane, R. W., Ibers, J. A., Frankel, R. B., Papaefthymiou, G. C., Holm, R. H., (1977) J. Am. Chem. Soc., 99, pp. 84-98
Benson, D. E., Wisz, M. S., Liu, W., Hellinga, H. W., (1998) Biochemistry, 37, pp. 7070-7076
Berg, J. M., Merkle, D. L., (1989) J. Am. Chem. Soc., 111, pp. 3759-3761
Krisek, B. A., Merkle, D. L., Berg, J. M., (1993) Inorg. Chem., 32, pp. 937-940
Fasman, G. D., (1996) Circular Dichroism and Conformationl Analysis of Biomolecules, , Plenum, New York
Miniaturized metalloproteins: Application to iron-sulfur proteins
The miniaturization process applied to rubredoxins generated a class of peptide-based metalloprotein models, named METP (miniaturized electron transfer protein). The crystal structure of Desulfovibrio vulgaris rubredoxin was selected as a template for the construction of a tetrahedral (S-gamma-Cys)(4) iron-binding site. Analysis of the structure showed that a sphere of 17 Angstrom in diameter, centered on the metal, circumscribes two unconnected approximately Ct symmetry related beta -hairpins, each containing the -Cys-(Aaa)(2)-Cys-sequence. These observations provided a starting point for the design Of an undecapeptide, which self assembles in the presence of tetrahedrally coordinating metal ions. The METP peptide was synthesized in good yield by standard methodologies. Successful assembly of the METP peptide with Co(II), Zn(II), Fe(II/III), in the expected 2:1 stoichiometry, was proven by UV-visible and circular dichroism spectroscopies. UV-visible analysis of the metal complexes indicated the four Cys ligands tetrahedrally arrange around the metal ion, as designed. Circular dichroism measurements on both the free and metal-bound forms revealed that the metal coordination drives the peptide chain to fold into a turned conformation. NMR characterization of the Zn(II)-METP complex fully supported the structure of the designed model. These results prove that METP reproduces the main features of rubredoxin.
Miniaturized metalloproteins: Application to iron-sulfur proteins
No results.
Miniaturized metalloproteins: Application to iron-sulfur proteins
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(357 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote