Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state (369 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10527-10535.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 8.091, 5-year impact factor: 8.256
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-49449107745&partnerID=40&md5=a4da15250f03fc8115ea5c72ed99fd0f
Keywords: Atomic Spectroscopy, Carbon Monoxide, Chemical Oxygen Demand, Iron, Leakage (fluid), Ligands, Nonmetals, Oxidation, Porphyrins, Allosteric Transition, Atomic Resolutions, Basic Concepts, Co Molecule, Crystallographic Characterization, Heme Iron, Intermediate Species, Oxidation Processes, Oxidation States, Oxidized States, Oxygen Release, Penta-Coordinated, Quaternary Structures, Spectroscopic Characterizations, Stereochemical Models, Structural Features, Structural Informations, Temporal Sequencing, Tertiary Structures, Hemoglobin, Iron Binding Protein, Tetramer, Alpha Chain, Antarctica, Article, Autooxidation, Beta Chain, Crystal Structure, Fish, Hemoglobin Determination, Phase Transition, Protein Binding, Protein Quaternary Structure, Protein Tertiary Structure, Stereochemistry, Structure Analysis, Animals, X-Ray, Fish Proteins, Oxidation-Reduction, Oxyhemoglobins, Perciformes, Protein Structure, Secondary, Spectrum Analysis,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Naples, Italy
Department of Chemistry, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, I-80126 Naples, Italy
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy
References:
Swain, J.F., Gierasch, L.M., (2006) Curr. Opin. Struct. Biol, 16, pp. 102-10
Gunasekaran, K., Ma, B., Nussinov, R., (2004) Proteins, 57, pp. 433-443
Kuriyan, J., Eisenberg, D., (2007) Nature, 450, pp. 983-990
Eaton, W.A., Henry, E.R., Hofrichter, J., Mozzarelli, A., (1999) Nat. Struct. Biol, 6, pp. 351-358
Bellelli, A., Brunori, M., Miele, A.E., Panetta, G., Vallone, B., (2006) Curr. Protein Pept. Sci, 7, pp. 17-45
Yonetani, T., Tsuneshige, A., (2003) C. R. Biol, 326, pp. 523-532
Barrick, D., Ho, N.T., Simplaceanu, V., Dahlquist, F.W., Ho, C., (1997) Nat. Struct. Biol, 4, pp. 78-83
Perutz, M.F., Wilkinson, A.J., Paoli, M., Dodson, G.G., (1998) Annu. Rev. Biophys. Biomol. Struct, 27, pp. 1-34
Perutz, M.F., (1970) Nature, 228, pp. 726-739
Safo, M.K., Abraham, D.J., (2005) Biochemistry, 44, pp. 8347-8359
Tame, J.R., (1999) Trends Biochem. Sci, 24, pp. 372-377
Silva, M.M., Rogers, P.H., Arnone, A., (1992) J. Biol. Chem, 267, pp. 17248-17256
Srinivasan, R., Rose, G.D., (1994) Proc. Natl. Acad. Sci. U.S.A, 91, pp. 11113-11117
Sutherland-Smith, A.J., Baker, H.M., Hofmann, O.M., Brittain, T., Baker, E.N., (1998) J. Mol. Biol, 280, pp. 475-484
Mueser, T.C., Rogers, P.H., Arnone, A., (2000) Biochemistry, 39, pp. 15353-15364
Schumacher, M.A., Zheleznova, E.E., Poundstone, K.S., Kluger, R., Jones, R.T., Brennan, R.G., (1997) Proc. Natl. Acad. Sci. U.S.A, 94, pp. 7841-7844
Schumacher, M.A., Dixon, M.M., Kluger, R., Jones, R.T., Brennan, R.G., (1995) Nature, 375, pp. 84-87
Kavanaugh, J.S., Rogers, P.H., Arnone, A., (2005) Biochemistry, 44, pp. 6101-6121
Park, S.Y., Yokoyama, T., Shibayama, N., Shiro, Y., Tame, J.R., (2006) J. Mol. Biol, 360, pp. 690-701
Viappiani, C., Bettati, S., Bruno, S., Ronda, L., Abbruzzetti, S., Mozzarelli, A., Eaton, W.A., (2004) Proc. Natl. Acad. Sci. U.S.A, 101, pp. 14414-14419
Woods, V. L., Jr Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 7057-7062Balakrishnan, G., Case, M.A., Pevsner, A., Zhao, X., Tengroth, C., McLendon, G.L., Spiro, T.G., (2004) J. Mol. Biol, 340, pp. 843-856
Jayaraman, V., Rodgers, K.R., Mukerji, I., Spiro, T.G., (1995) Science, 269, pp. 1843-1848
Lukin, J.A., Kontaxis, G., Simplaceanu, V., Yuan, Y., Bax, A., Ho, C., (2003) Proc. Natl. Acad. Sci. U.S.A, 100, pp. 517-520
Knapp, J.E., Pahl, R., Srajer, V., Royer Jr., W.E., (2006) Proc. Natl. Acad. Sci. U.S.A, 103, pp. 7649-7654
Bourgeois, D., Vallone, B., Arcovito, A., Sciara, G., Schotte, F., Anfinrud, P.A., Brunori, M., (2006) Proc. Natl. Acad. Sci. U.S.A, 103, pp. 4924-4929
Schmidt, M., Nienhaus, K., Pahl, R., Krasselt, A., Anderson, S., Parak, F., Nienhaus, G.U., Srajer, V., (2005) Proc. Natl. Acad. Sci. U.S.A, 102, pp. 11704-11709
Ostermann, A., Waschipky, R., Parak, F.G., Nienhaus, G.U., (2000) Nature, 404, pp. 205-208
Adachi, S., Park, S.Y., Tame, J.R., Shiro, Y., Shibayama, N., (2003) Proc. Natl. Acad. Sci. U.S.A, 100, pp. 7039-7044
Vitagliano, L., Bonomi, G., Riccio, A., di Prisco, G., Smulevich, G., Mazzarella, L., (2004) Eur. J. Biochem, 271, pp. 1651-1659
Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A., Mazzarella, L., (2002) Proc. Natl. Acad. Sci. U.S.A, 99, pp. 9801-9806
Vergara, A., Franzese, M., Merlino, A., Vitagliano, L., Verde, C., di Prisco, G., Lee, H.C., Mazzarella, L., (2007) Biophys. J, 93, pp. 2822-2829
D'Avino, R., Caruso, C., Tamburrini, M., Romano, M., Rutigliano, B., Polverino de Laureto, P., Camardella, L., di Prisco, G., (1994) J. Biol. Chem, 269, pp. 9675-9681
Otwinowsky, Z., Minor, W., (1997) Methods Enzymol, 276, pp. 307-326
Navaza, J., (1994) Acta Crystallogr., Sect. A: Found. Crystallogr, A50, pp. 157-163
Mazzarella, L., D'Avino, R., di Prisco, G., Savino, C., Vitagliano, L., Moody, P.C., Zagari, A., (1999) J. Mol. Biol, 287, pp. 897-906
Sheldrick, G.M., Schneider, T.R., (1997) Methods Enzymol, 277, pp. 319-343
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., (1991) Acta Crystallogr., Sect. A: Found. Crystallogr, 47, pp. 110-119
Laskowski, R.A., MacArthur, M.W., Moss, M.D., Thorton, J.M., (1993) J. Appl. Crystallogr, 26, pp. 283-291
Droghetti, E., Howes, B.D., Feis, A., Dominici, P., Fittipaldi, M., Smulevich, G., (2007) J. Inorg. Biochem, 101, pp. 1812-1819
Spiro, T.G., (1985) Adv. Protein Chem, 37, pp. 111-159
Kitagawa, T., Nagai, K., Tsubaki, M., (1979) FEBS Lett, 104, pp. 376-378
Mazzarella, L., Vergara, A., Vitagliano, L., Merlino, A., Bonomi, G., Scala, S., Verde, C., di Prisco, G., (2006) Proteins, 65, pp. 490-498
Mazzarella, L., Bonomi, G., Lubrano, M.C., Merlino, A., Riccio, A., Vergara, A., Vitagliano, L., di Prisco, G., (2006) Proteins, 62, pp. 316-321
Wilson, J., Phillips, K., Luisi, B., (1996) J. Mol. Biol, 264, pp. 743-756
Giordano, D., Vergara, A., Lee, H.C., Peisach, J., Balestrieri, M., Mazzarella, L., Parisi, E., Verde, C., (2007) Gene, 406, pp. 58-68
Smulevich, G., (1998) Biospectroscopy, 4, pp. S3-17
Edelstein, S.J., (1996) J. Mol. Biol, 257, pp. 737-744
Safo, M.K., Burnett, J.C., Musayev, F.N., Nokuri, S., Abraham, D.J., (2002) Acta Crystallogr., Sect. D: Biol. Crystallogr, 58, pp. 2031-2037
Paoli, M., Liddington, R., Tame, J., Wilkinson, A., Dodson, G., (1996) J. Mol. Biol, 256, pp. 775-792
Park, S.Y., Shibayama, N., Hiraki, T., Tame, J.R., (2004) Biochemistry, 43, pp. 8711-8717
Shibayama, N., Miura, S., Tame, J.R., Yonetani, T., Park, S.Y., (2002) J. Biol. Chem, 277, pp. 38791-38796
Luisi, B., Liddington, B., Fermi, G., Shibayama, N., (1990) J. Mol. Biol, 214, pp. 7-14
Swain, J. F., Gierasch, L. M., (2006) Curr. Opin. Struct. Biol, 16, pp. 102-10
Eaton, W. A., Henry, E. R., Hofrichter, J., Mozzarelli, A., (1999) Nat. Struct. Biol, 6, pp. 351-358
Perutz, M. F., Wilkinson, A. J., Paoli, M., Dodson, G. G., (1998) Annu. Rev. Biophys. Biomol. Struct, 27, pp. 1-34
Perutz, M. F., (1970) Nature, 228, pp. 726-739
Safo, M. K., Abraham, D. J., (2005) Biochemistry, 44, pp. 8347-8359
Tame, J. R., (1999) Trends Biochem. Sci, 24, pp. 372-377
Silva, M. M., Rogers, P. H., Arnone, A., (1992) J. Biol. Chem, 267, pp. 17248-17256
Mueser, T. C., Rogers, P. H., Arnone, A., (2000) Biochemistry, 39, pp. 15353-15364
Schumacher, M. A., Zheleznova, E. E., Poundstone, K. S., Kluger, R., Jones, R. T., Brennan, R. G., (1997) Proc. Natl. Acad. Sci. U. S. A, 94, pp. 7841-7844
Kavanaugh, J. S., Rogers, P. H., Arnone, A., (2005) Biochemistry, 44, pp. 6101-6121
Park, S. Y., Yokoyama, T., Shibayama, N., Shiro, Y., Tame, J. R., (2006) J. Mol. Biol, 360, pp. 690-701
Lukin, J. A., Kontaxis, G., Simplaceanu, V., Yuan, Y., Bax, A., Ho, C., (2003) Proc. Natl. Acad. Sci. U. S. A, 100, pp. 517-520
Knapp, J. E., Pahl, R., Srajer, V., Royer Jr., W. E., (2006) Proc. Natl. Acad. Sci. U. S. A, 103, pp. 7649-7654
Sheldrick, G. M., Schneider, T. R., (1997) Methods Enzymol, 277, pp. 319-343
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., (1991) Acta Crystallogr., Sect. A: Found. Crystallogr, 47, pp. 110-119
Laskowski, R. A., MacArthur, M. W., Moss, M. D., Thorton, J. M., (1993) J. Appl. Crystallogr, 26, pp. 283-291
Spiro, T. G., (1985) Adv. Protein Chem, 37, pp. 111-159
Edelstein, S. J., (1996) J. Mol. Biol, 257, pp. 737-744
Safo, M. K., Burnett, J. C., Musayev, F. N., Nokuri, S., Abraham, D. J., (2002) Acta Crystallogr., Sect. D: Biol. Crystallogr, 58, pp. 2031-2037
Park, S. Y., Shibayama, N., Hiraki, T., Tame, J. R., (2004) Biochemistry, 43, pp. 8711-8717
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10527-10535.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 8.091, 5-year impact factor: 8.256
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-49449107745&partnerID=40&md5=a4da15250f03fc8115ea5c72ed99fd0f
Keywords: Atomic Spectroscopy, Carbon Monoxide, Chemical Oxygen Demand, Iron, Leakage (fluid), Ligands, Nonmetals, Oxidation, Porphyrins, Allosteric Transition, Atomic Resolutions, Basic Concepts, Co Molecule, Crystallographic Characterization, Heme Iron, Intermediate Species, Oxidation Processes, Oxidation States, Oxidized States, Oxygen Release, Penta-Coordinated, Quaternary Structures, Spectroscopic Characterizations, Stereochemical Models, Structural Features, Structural Informations, Temporal Sequencing, Tertiary Structures, Hemoglobin, Iron Binding Protein, Tetramer, Alpha Chain, Antarctica, Article, Autooxidation, Beta Chain, Crystal Structure, Fish, Hemoglobin Determination, Phase Transition, Protein Binding, Protein Quaternary Structure, Protein Tertiary Structure, Stereochemistry, Structure Analysis, Animals, X-Ray, Fish Proteins, Oxidation-Reduction, Oxyhemoglobins, Perciformes, Protein Structure, Secondary, Spectrum Analysis,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Naples, Italy
Department of Chemistry, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, I-80126 Naples, Italy
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy
References:
Swain, J.F., Gierasch, L.M., (2006) Curr. Opin. Struct. Biol, 16, pp. 102-10
Gunasekaran, K., Ma, B., Nussinov, R., (2004) Proteins, 57, pp. 433-443
Kuriyan, J., Eisenberg, D., (2007) Nature, 450, pp. 983-990
Eaton, W.A., Henry, E.R., Hofrichter, J., Mozzarelli, A., (1999) Nat. Struct. Biol, 6, pp. 351-358
Bellelli, A., Brunori, M., Miele, A.E., Panetta, G., Vallone, B., (2006) Curr. Protein Pept. Sci, 7, pp. 17-45
Yonetani, T., Tsuneshige, A., (2003) C. R. Biol, 326, pp. 523-532
Barrick, D., Ho, N.T., Simplaceanu, V., Dahlquist, F.W., Ho, C., (1997) Nat. Struct. Biol, 4, pp. 78-83
Perutz, M.F., Wilkinson, A.J., Paoli, M., Dodson, G.G., (1998) Annu. Rev. Biophys. Biomol. Struct, 27, pp. 1-34
Perutz, M.F., (1970) Nature, 228, pp. 726-739
Safo, M.K., Abraham, D.J., (2005) Biochemistry, 44, pp. 8347-8359
Tame, J.R., (1999) Trends Biochem. Sci, 24, pp. 372-377
Silva, M.M., Rogers, P.H., Arnone, A., (1992) J. Biol. Chem, 267, pp. 17248-17256
Srinivasan, R., Rose, G.D., (1994) Proc. Natl. Acad. Sci. U.S.A, 91, pp. 11113-11117
Sutherland-Smith, A.J., Baker, H.M., Hofmann, O.M., Brittain, T., Baker, E.N., (1998) J. Mol. Biol, 280, pp. 475-484
Mueser, T.C., Rogers, P.H., Arnone, A., (2000) Biochemistry, 39, pp. 15353-15364
Schumacher, M.A., Zheleznova, E.E., Poundstone, K.S., Kluger, R., Jones, R.T., Brennan, R.G., (1997) Proc. Natl. Acad. Sci. U.S.A, 94, pp. 7841-7844
Schumacher, M.A., Dixon, M.M., Kluger, R., Jones, R.T., Brennan, R.G., (1995) Nature, 375, pp. 84-87
Kavanaugh, J.S., Rogers, P.H., Arnone, A., (2005) Biochemistry, 44, pp. 6101-6121
Park, S.Y., Yokoyama, T., Shibayama, N., Shiro, Y., Tame, J.R., (2006) J. Mol. Biol, 360, pp. 690-701
Viappiani, C., Bettati, S., Bruno, S., Ronda, L., Abbruzzetti, S., Mozzarelli, A., Eaton, W.A., (2004) Proc. Natl. Acad. Sci. U.S.A, 101, pp. 14414-14419
Woods, V. L., Jr Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 7057-7062Balakrishnan, G., Case, M.A., Pevsner, A., Zhao, X., Tengroth, C., McLendon, G.L., Spiro, T.G., (2004) J. Mol. Biol, 340, pp. 843-856
Jayaraman, V., Rodgers, K.R., Mukerji, I., Spiro, T.G., (1995) Science, 269, pp. 1843-1848
Lukin, J.A., Kontaxis, G., Simplaceanu, V., Yuan, Y., Bax, A., Ho, C., (2003) Proc. Natl. Acad. Sci. U.S.A, 100, pp. 517-520
Knapp, J.E., Pahl, R., Srajer, V., Royer Jr., W.E., (2006) Proc. Natl. Acad. Sci. U.S.A, 103, pp. 7649-7654
Bourgeois, D., Vallone, B., Arcovito, A., Sciara, G., Schotte, F., Anfinrud, P.A., Brunori, M., (2006) Proc. Natl. Acad. Sci. U.S.A, 103, pp. 4924-4929
Schmidt, M., Nienhaus, K., Pahl, R., Krasselt, A., Anderson, S., Parak, F., Nienhaus, G.U., Srajer, V., (2005) Proc. Natl. Acad. Sci. U.S.A, 102, pp. 11704-11709
Ostermann, A., Waschipky, R., Parak, F.G., Nienhaus, G.U., (2000) Nature, 404, pp. 205-208
Adachi, S., Park, S.Y., Tame, J.R., Shiro, Y., Shibayama, N., (2003) Proc. Natl. Acad. Sci. U.S.A, 100, pp. 7039-7044
Vitagliano, L., Bonomi, G., Riccio, A., di Prisco, G., Smulevich, G., Mazzarella, L., (2004) Eur. J. Biochem, 271, pp. 1651-1659
Riccio, A., Vitagliano, L., di Prisco, G., Zagari, A., Mazzarella, L., (2002) Proc. Natl. Acad. Sci. U.S.A, 99, pp. 9801-9806
Vergara, A., Franzese, M., Merlino, A., Vitagliano, L., Verde, C., di Prisco, G., Lee, H.C., Mazzarella, L., (2007) Biophys. J, 93, pp. 2822-2829
D'Avino, R., Caruso, C., Tamburrini, M., Romano, M., Rutigliano, B., Polverino de Laureto, P., Camardella, L., di Prisco, G., (1994) J. Biol. Chem, 269, pp. 9675-9681
Otwinowsky, Z., Minor, W., (1997) Methods Enzymol, 276, pp. 307-326
Navaza, J., (1994) Acta Crystallogr., Sect. A: Found. Crystallogr, A50, pp. 157-163
Mazzarella, L., D'Avino, R., di Prisco, G., Savino, C., Vitagliano, L., Moody, P.C., Zagari, A., (1999) J. Mol. Biol, 287, pp. 897-906
Sheldrick, G.M., Schneider, T.R., (1997) Methods Enzymol, 277, pp. 319-343
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., (1991) Acta Crystallogr., Sect. A: Found. Crystallogr, 47, pp. 110-119
Laskowski, R.A., MacArthur, M.W., Moss, M.D., Thorton, J.M., (1993) J. Appl. Crystallogr, 26, pp. 283-291
Droghetti, E., Howes, B.D., Feis, A., Dominici, P., Fittipaldi, M., Smulevich, G., (2007) J. Inorg. Biochem, 101, pp. 1812-1819
Spiro, T.G., (1985) Adv. Protein Chem, 37, pp. 111-159
Kitagawa, T., Nagai, K., Tsubaki, M., (1979) FEBS Lett, 104, pp. 376-378
Mazzarella, L., Vergara, A., Vitagliano, L., Merlino, A., Bonomi, G., Scala, S., Verde, C., di Prisco, G., (2006) Proteins, 65, pp. 490-498
Mazzarella, L., Bonomi, G., Lubrano, M.C., Merlino, A., Riccio, A., Vergara, A., Vitagliano, L., di Prisco, G., (2006) Proteins, 62, pp. 316-321
Wilson, J., Phillips, K., Luisi, B., (1996) J. Mol. Biol, 264, pp. 743-756
Giordano, D., Vergara, A., Lee, H.C., Peisach, J., Balestrieri, M., Mazzarella, L., Parisi, E., Verde, C., (2007) Gene, 406, pp. 58-68
Smulevich, G., (1998) Biospectroscopy, 4, pp. S3-17
Edelstein, S.J., (1996) J. Mol. Biol, 257, pp. 737-744
Safo, M.K., Burnett, J.C., Musayev, F.N., Nokuri, S., Abraham, D.J., (2002) Acta Crystallogr., Sect. D: Biol. Crystallogr, 58, pp. 2031-2037
Paoli, M., Liddington, R., Tame, J., Wilkinson, A., Dodson, G., (1996) J. Mol. Biol, 256, pp. 775-792
Park, S.Y., Shibayama, N., Hiraki, T., Tame, J.R., (2004) Biochemistry, 43, pp. 8711-8717
Shibayama, N., Miura, S., Tame, J.R., Yonetani, T., Park, S.Y., (2002) J. Biol. Chem, 277, pp. 38791-38796
Luisi, B., Liddington, B., Fermi, G., Shibayama, N., (1990) J. Mol. Biol, 214, pp. 7-14
Swain, J. F., Gierasch, L. M., (2006) Curr. Opin. Struct. Biol, 16, pp. 102-10
Eaton, W. A., Henry, E. R., Hofrichter, J., Mozzarelli, A., (1999) Nat. Struct. Biol, 6, pp. 351-358
Perutz, M. F., Wilkinson, A. J., Paoli, M., Dodson, G. G., (1998) Annu. Rev. Biophys. Biomol. Struct, 27, pp. 1-34
Perutz, M. F., (1970) Nature, 228, pp. 726-739
Safo, M. K., Abraham, D. J., (2005) Biochemistry, 44, pp. 8347-8359
Tame, J. R., (1999) Trends Biochem. Sci, 24, pp. 372-377
Silva, M. M., Rogers, P. H., Arnone, A., (1992) J. Biol. Chem, 267, pp. 17248-17256
Mueser, T. C., Rogers, P. H., Arnone, A., (2000) Biochemistry, 39, pp. 15353-15364
Schumacher, M. A., Zheleznova, E. E., Poundstone, K. S., Kluger, R., Jones, R. T., Brennan, R. G., (1997) Proc. Natl. Acad. Sci. U. S. A, 94, pp. 7841-7844
Kavanaugh, J. S., Rogers, P. H., Arnone, A., (2005) Biochemistry, 44, pp. 6101-6121
Park, S. Y., Yokoyama, T., Shibayama, N., Shiro, Y., Tame, J. R., (2006) J. Mol. Biol, 360, pp. 690-701
Lukin, J. A., Kontaxis, G., Simplaceanu, V., Yuan, Y., Bax, A., Ho, C., (2003) Proc. Natl. Acad. Sci. U. S. A, 100, pp. 517-520
Knapp, J. E., Pahl, R., Srajer, V., Royer Jr., W. E., (2006) Proc. Natl. Acad. Sci. U. S. A, 103, pp. 7649-7654
Sheldrick, G. M., Schneider, T. R., (1997) Methods Enzymol, 277, pp. 319-343
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., (1991) Acta Crystallogr., Sect. A: Found. Crystallogr, 47, pp. 110-119
Laskowski, R. A., MacArthur, M. W., Moss, M. D., Thorton, J. M., (1993) J. Appl. Crystallogr, 26, pp. 283-291
Spiro, T. G., (1985) Adv. Protein Chem, 37, pp. 111-159
Edelstein, S. J., (1996) J. Mol. Biol, 257, pp. 737-744
Safo, M. K., Burnett, J. C., Musayev, F. N., Nokuri, S., Abraham, D. J., (2002) Acta Crystallogr., Sect. D: Biol. Crystallogr, 58, pp. 2031-2037
Park, S. Y., Shibayama, N., Hiraki, T., Tame, J. R., (2004) Biochemistry, 43, pp. 8711-8717
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state
Tetrameric hemoglobins represent the most commonly used model for the description of the basic concepts of protein allostery. The classical stereochemical model assumes a concerted transition of the protein, upon oxygen release, from the relaxed (R) to the tense (T) state. Despite the large amount of data accumulated on the end-points of the transition, scarce structural information is available on the intermediate species along the pathway. Here we report a spectroscopic characterization of the autoxidation process of the Trematomus newnesi major Hb component and the atomic resolution structure (1.25 angstrom) of an intermediate form along the pathway characterized by a different binding and oxidation state of the a and beta chains. In contrast to the alpha-heme iron, which binds a CO molecule, the beta iron displays a pentacoordinated oxidized state, which is rare in tetrameric hemoglobins. Interestingly, the information provided by the present analysis is not limited to the characterization of the peculiar oxidation process of Antarctic fish hemoglobins. Indeed, this structure represents the most detailed snapshot of hemoglobin allosteric transition hitherto achieved. Upon ligand release at the beta heme, a cascade of structural events is observed. Notably, several structural features of the tertiary structure of the alpha and beta chains closely resemble those typically observed in the deoxygenated state. The overall quaternary structure also becomes intermediate between the R and the T state. The analysis of the alterations induced by the ligand release provides a clear picture of the temporal sequence of the events associated with the transition. The implications of the present findings have also been discussed in the wider context of tetrameric Hbs.
Tetrameric hemoglobins represent the most commonly used model for the description of the basic concepts of protein allostery. The classical stereochemical model assumes a concerted transition of the protein, upon oxygen release, from the relaxed (R) to the tense (T) state. Despite the large amount of data accumulated on the end-points of the transition, scarce structural information is available on the intermediate species along the pathway. Here we report a spectroscopic characterization of the autoxidation process of the Trematomus newnesi major Hb component and the atomic resolution structure (1.25 angstrom) of an intermediate form along the pathway characterized by a different binding and oxidation state of the a and beta chains. In contrast to the alpha-heme iron, which binds a CO molecule, the beta iron displays a pentacoordinated oxidized state, which is rare in tetrameric hemoglobins. Interestingly, the information provided by the present analysis is not limited to the characterization of the peculiar oxidation process of Antarctic fish hemoglobins. Indeed, this structure represents the most detailed snapshot of hemoglobin allosteric transition hitherto achieved. Upon ligand release at the beta heme, a cascade of structural events is observed. Notably, several structural features of the tertiary structure of the alpha and beta chains closely resemble those typically observed in the deoxygenated state. The overall quaternary structure also becomes intermediate between the R and the T state. The analysis of the alterations induced by the ligand release provides a clear picture of the temporal sequence of the events associated with the transition. The implications of the present findings have also been discussed in the wider context of tetrameric Hbs.
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state
| ▼ Structural characterization of the porphyrins/proteasome interaction |
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state
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* Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages (210 views)
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View Export to BibTeX Export to EndNote
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Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2018; 24(24): 6349-6353.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Santoro AM, Cunsolo A, D'Urso A, Sbardella D, Tundo GR, Ciaccio C, Coletta M, Diana D, Fattorusso R, Persico M, Di Dato A, Fattorusso C, Milardi D, Purrello R
* Cationic porphyrins are tunable gatekeepers of the 20S proteasome (638 views) (PDF 228 views)
Chem Sci (ISSN: 2041-6520, 2041-6520linking, 2041-6520print), 2016; 7(2): 1286-1297.
Impact Factor: 8.668
View Export to BibTeX Export to EndNote
Vitale R, Lista L, Cerrone C, Caserta G, Chino M, Maglio O, Nastri F, Pavone V, Lombardi A
* An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization (415 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
Impact Factor: 3.559
View Export to BibTeX Export to EndNote
Engelen M, Lombardi A, Vitale R, Lista L, Maglio O, Pavone V, Nastri F
* Branched porphyrins as functional scaffolds for multisite bioconjugation (334 views)
Biotechnol Appl Bioc (ISSN: 0885-4513), 2014 Sep 21; N/D: N/D-N/D.
Impact Factor: 1.362
View Export to BibTeX Export to EndNote
Coppola D, Abbruzzetti S, Nicoletti F, Merlino A, Gambacurta A, Giordano D, Howes BD, De Sanctis G, Vitagliano L, Bruno S, di Prisco G, Mazzarella L, Smulevich G, Coletta M, Viappiani C, Vergara A, Verde C
* ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus (310 views)
Molecular Biosystems (ISSN: 1742-206x), 2012 Oct 30; 8(12): 3295-3304.
Impact Factor: 3.35
View Export to BibTeX Export to EndNote
Santoro AM, Lo Giudice MC, D'Urso A, Lauceri R, Purrello R, Milardi D
* Cationic porphyrins are reversible proteasome inhibitors (436 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2012 Jun 27; 134(25): 10451-10457.
Impact Factor: 10.677
View Export to BibTeX Export to EndNote
Tabbì G, Di Mauro G, Purrello R, Bonomo RP
* Electrochemical characterization of ordered arrays of metallo-porphyrins in aqueous solution (344 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2011 Apr 28; 40(16): 4223-4229.
Impact Factor: 3.838
View Export to BibTeX Export to EndNote
Nastri F, Lista L, Ringhieri P, Vitale R, Faiella M, Andreozzi C, Travascio P, Maglio O, Lombardi A, Pavone V
* A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity (421 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
Impact Factor: 5.925
View Export to BibTeX Export to EndNote
La Mendola D, Magrì A, Vagliasindi LI, Hansson Ö, Bonomo RP, Rizzarelli E
* Copper(II) complex formation with a linear peptide encompassing the putative cell binding site of angiogenin (433 views)
Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2010 Nov 28; 39(44): 10678-10684.
Impact Factor: 3.647
View Export to BibTeX Export to EndNote
Vergara A, Vitagliano L, Merlino A, Sica F, Marino K, Verde C, di Prisco G, Mazzarella L
* An Order-Disorder Transition Plays a Role in Switching Off the Root Effect in Fish Hemoglobins (343 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2010 Oct 15; 285(42): 32568-32575.
Impact Factor: 5.328
View Export to BibTeX Export to EndNote
Merlino A, Vergara A, Sica F, Aschi M, Amadei A, Di Nola A, Mazzarella L
* Free-Energy Profile for CO Binding to Separated Chains of Human and Trematomus newnesi Hemoglobin: Insights from Molecular Dynamics Simulations and Perturbed Matrix Method (290 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 May 27; 114(20): 7002-7008.
Impact Factor: 3.603
View Export to BibTeX Export to EndNote
Merlino A, Vitagliano L, Howes BD, Verde C, Di Prisco G, Smulevich G, Sica F, Vergara A
* Combined Crystallographic and Spectroscopic Analysis of Trematomus bernacchii Hemoglobin Highlights Analogies and Differences in the Peculiar Oxidation Pathway of Antarctic Fish Hemoglobins (379 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
View Export to BibTeX Export to EndNote
Randazzo R, Lauceri R, Mammana A, D'Urso A, Purrello R
* Interactions of Λ and Δ enantiomers of ruthenium(II) cationic complexes with achiral anionic porphyrins (343 views)
Chirality (ISSN: 0899-0042), 2009; 21(1): 92-96.
Impact Factor: 2.677
View Export to BibTeX Export to EndNote
Lauceri R, Fasciglione G, D'Urso A, Marini S, Purrello R, Coletta M
* Kinetic investigation of porphyrin interaction with chiral templates reveals unexpected features of the induction and self-propagation mechanism of chiral memory (395 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10476-10477.
Impact Factor: 8.091
View Export to BibTeX Export to EndNote
Randazzo R, Mammana A, D'Urso A, Lauceri R, Purrello R
* Reversible "chiral memory" in ruthenium tris(phenanthroline)- anionic porphyrin complexes (391 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2008; 47(51): 9879-9882.
Impact Factor: 10.879
View Export to BibTeX Export to EndNote
Castiglioni E, Abbate S, Longhi G, Gangemi R, Lauceri R, Purrello R
* Absorption flattening as one cause of distortion of circular dichroism spectra of Δ-RuPhen3·H2TPPS complex (294 views)
Chirality (ISSN: 0899-0042), 2007 Sep; 19(8): 642-646.
Impact Factor: 2.436
View Export to BibTeX Export to EndNote
Matassa R, Carbone M, Lauceri R, Purrello R, Caminiti R
* Supramolecular structure of extrinsically chiral porphyrin hetero-assemblies and achiral analogues (309 views)
Adv Mater (ISSN: 0935-9648), 2007; 19(22): 3961-3967.
Impact Factor: 8.191
View Export to BibTeX Export to EndNote
Angela M, Massimo De N, Rosaria L, Roberto P
* Induction and memory of chirality in porphyrin hetero-aggregates: The role of the central metal ion (403 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 1464-3391electronic), 2005 Sep 1; 13(17): 5159-5163.
Impact Factor: 2.286
View Export to BibTeX Export to EndNote
Lauceria R, Purrellob R
* Transfer, memory and amplification of chirality in porphyrin aggregates (293 views)
Supramol Chem (ISSN: 1061-0278), 2005; 17(1-2): 61-66.
Impact Factor: 1.715
View Export to BibTeX Export to EndNote
Di Costanzo L, Geremia S, Randaccio L, Nastri F, Maglio O, Lombardi A, Pavone V
* Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV (355 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2004 Dec; 9(8): 1017-1027.
Impact Factor: 3.3
View Export to BibTeX Export to EndNote
Clemente F, D'Avino E, Guaragno M, Menichetti A
* An on line technique to detect cardiac output variations and cardiovascular performances during abdominal aortic surgery (436 views)
Journal Of Clinical Monitoring And Computing (ISSN: 1387-1307), 2004 Apr; 18(2): 81-87.
Impact Factor: 0.888
View Export to BibTeX Export to EndNote
Moschetto A, Lauceri R, Gulino FG, Sciotto D, Purrello R
* Non-covalent synthesis in aqueous solution of discrete multi-porphyrin aggregates with programmable stoichiometry and sequence (398 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2002 Dec 11; 124(49): 14536-14537.
Impact Factor: 6.201
View Export to BibTeX Export to EndNote
Lauceri R, Raudino A, Scolaro LM, Micali N, Purrello R
* From achiral porphyrins to template-imprinted chiral aggregates and further. Self-replication of chiral memory from scratch (492 views)
J Am Chem Soc (ISSN: 0002-7863print, 0002-7863linking, 1520-5126electronic), 2002 Feb 13; 120(47): 894-895.
Impact Factor: 9.023
View Export to BibTeX Export to EndNote
Lauceri R, Purrello R, Shetty SJ, Vicente MGH
* Interactions of anionic carboranylated porphyrins with DNA [3] (301 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2001 Jun 20; 123(24): 5835-5836.
Impact Factor: 6.079
View Export to BibTeX Export to EndNote
Aime S, Dastrù W, Gobetto R, Viale A
An NMR study of H(μ-H)Os3(CO)11 (349 views)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2000; 39(11): 2422-2425.
Impact Factor: 2.712
View Export to BibTeX Export to EndNote
De Luca S, Bruno G, Fattorusso R, Isernia C, Pedone C, Morelli G
New synthetic tools for peptide-tetraphenylporphyrin derivatives (300 views)
Int J Pept Res Ther (ISSN: 0929-5666, 1573-3149), 1998 Jul; 5(4): 269-276.
Impact Factor: 0.557
View Export to BibTeX Export to EndNote
Nastri F, Lombardi A, D'Andrea LD, Sanseverino M, Maglio O, Pavone V
Miniaturized hemoproteins (399 views)
Biopolymers (ISSN: 0006-3525print, 0006-3525linking, 1097-0282electronic), 1998; 47(1): 5-22.
Impact Factor: 2.086
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Purrello R, Bellacchio E, Gurrieri S, Lauceri R, Raudino A, Monsù Scolaro L, Santoro AM
Ph Modulation Of Porphyrins Self-Assembly Onto Polylisine (218 views)
Journal Of Physical Chemistry B, 1998; N/D: 8852-8857.
Impact Factor: 0
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Colasanti A, Kisslinger A, Kusch D, Liuzzi R, Mastrocinque M, Montforts FP, Quarto M, Riccio P, Roberti G, Villani F
In vitro photo-activation of newly synthesized chlorin derivatives with red-light-emitting diodes (317 views)
J Photochem Photobiol B (ISSN: 1011-1344print, 1011-1344linking), 1997 Mar; 38(1): 54-60.
Impact Factor: 1.381
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Mastruzzo L, Woisard A, Ma DD, Rizzarelli E, Favre A, Le Doan T
TARGETED PHOTOCHEMICAL MODIFICATION OF HIV-DERIVED OLIGORIBONUCLEOTIDES BY ANTISENSE OLIGODEOXYNUCLEOTIDES LINKED TO PORPHYRINS (267 views)
Photochem Photobiol (ISSN: 0031-8655), 1994 Oct; 60(4): 316-322.
Impact Factor: 2.426
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Bustamante C, Gurrieri S, Pasternack RF, Purrello R, Rizzarelli E
Interaction of water-soluble porphyrins with single- and double-stranded polyribonucleotides (387 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Sep; 34(8): 1099-1104.
Impact Factor: 2.425
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33 Records (33 excluding Abstracts).
Total impact factor: 133.963 (133.963 excluding Abstracts).
Total 5 year impact factor: 150.56 (150.56 excluding Abstracts).
Total impact factor: 133.963 (133.963 excluding Abstracts).
Total 5 year impact factor: 150.56 (150.56 excluding Abstracts).
369 views. Last view on Tuesday 20 September 2022, 3:35:54
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