Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin (287 views)
Rsc Adv (ISSN: 2046-2069), 2014; 4(49): 25852-25856.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.84, 5-year impact factor: 3.907
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84902981233&partnerID=40&md5=b1893d2203b1f9f47a4151ee0d690c58
Keywords: Cyanidation, Haemoglobins, Structural Modifications, Tetrameric, X Ray Crystal Structures,
Affiliations:
*** IBB - CNR ***
Dept of Chemical Sciences, University of Naples Federico II, Naples, Italy
Institute of Biostructures and Bioimaging, CNR, Naples, Italy
Institute of Biosciences and BioResources, CNR, Naples, Italy
Roma 3 University, Dept of Biology, Rome, Italy
Dept of Biophysics and Physiology, Albert Einstein College of Medicine, New York NY, United States
References:
Kakar, S., Hoffman, F.G., Storz, J.F., Fabian, M., Hargrove, M.S., (2010) Biophys. Chem., 152, p.
Merlino, A., Howes, B., Verde, C., Di Prisco, G., Smulevich, G., Mazzarella, L., Vergara, A., (2011) IUBMB Life, 63, p. 295
Wittenberg, J., Wittenberg, B., Gibson, Q., Trinick, M., Appleby, C., (1986) J. Biol. Chem., 261, p. 13624
Weiland, T.R., Kundu, S., Trent III, J.T., Hoy, J.A., Hargrove, M.S., (2004) J. Am. Chem. Soc., 126, p. 11930
Rifkind, J.M., Abugo, O., Levy, A., Heim, J.M., (1994) Methods Enzymol., 231, p. 449
Pesce, A., De Sanctis, D., Nardini, M., Dewilde, S., Moens, L., Hankeln, T., Burmester, T., Bolognesi, M., (2004) IUBMB Life, 56, p. 657
Tokumasu, F., Nardone, G.A., Ostera, G.R., Fairhurst, R.M., Beaudry, S.D., Hayakawa, E., Dvorak, J.A., (2009) PLoS One, 4, p. 1
Vergara, A., Franzese, M., Merlino, A., Bonomi, G., Verde, C., Giordano, D., Di Prisco, G., Mazzarella, L., (2009) Biophys. J., 97, p. 866
Robinson, V.L., Smith, B.B., Arnone, A., (2003) Biochemistry, 42, p. 10113
Ramesh, P., Sundaresan, S.S., Moorthy, P.S., Balasubramanian, M., Ponnnuswamy, M.N., (2013) J. Synchrotron Radiat., 20, p. 843
Ronda, L., Merlino, A., Bettati, S., Verde, C., Balsamo, A., Mazzarella, L., Mozzarelli, A., Vergara, A., (2013) Biochim. Biophys. Acta, Proteins Proteomics, 1834, p. 1885
Balsamo, A., Sannino, F., Merlino, A., Parrilli, E., Tutino, M.L., Mazzarella, L., Vergara, A., (2012) Biochimie, 94, p. 953
Rachmilewitz, E.A., Peisach, J., Blumberg, W.E., (1971) J. Biol. Chem., 246, p. 3356
Trent III, J.T., Kundu, S., Hoy, J.A., Hargrove, M.S., (2004) J. Mol. Biol., 341, p. 1097
De Sanctis, D., Ascenzi, P., Bocedi, A., Dewilde, S., Burmester, T., Hankeln, T., Moens, L., Bolognesi, M., (2006) Biochemistry, 45, p. 10054
Mitchell, D.T., Kitto, G.B., Hackert, M.L., (1995) J. Mol. Biol., 251, p. 421
Otwinowski, Z., Minor, W., (1997) Methods Enzymol., 276 (PART A), p. 307
Sheldrick, G.M., (2008) Acta Crystallogr., Sect. D: Biol. Crystallogr., 64, p. 112
Jones, T.A., Kjeldgaard, M., (1988) Essential O, Software Manual, , Uppsala, p. 178
Vergara, A., Vitagliano, L., Verde, C., Di Prisco, G., Mazzarella, L., (2008) Methods Enzymol., 436 (425), p. 56
Camardella, L., Caruso, C., D'Avino, R., Di Prisco, G., Rutigliano, B., Tamburrini, M., Fermi, G., Perutz, M.F., (1992) J. Mol. Biol., 224, p. 449
Verde, C., Vergara, A., Mazzarella, L., Di Prisco, G., (2008) Curr. Protein Pept. Sci., 9, p. 578
Vitagliano, L., Vergara, A., Bonomi, G., Merlino, A., Verde, C., Di Prisco, G., Howes, B.D., Mazzarella, L., (2008) J. Am. Chem. Soc., 130, p. 10527
Merlino, A., Vitagliano, L., Howes, B.D., Verde, C., Di Prisco, G., Smulevich, G., Sica, F., Vergara, A., (2009) Biopolymers, 91, p. 1117
Capece, L., Boechi, L., Perissinotti, L.L., Arroyo-Mañez, P., Bikiel, D.E., Smulevich, G., Marti, M.A., Estrin, D.A., (2013) Biochim. Biophys. Acta, 1834 (1722), p. 57
Jenkins, J.D., Musayev, F.N., Danso-Danquah, R., Abraham, D.J., Safo, M.K., (2009) Acta Crystallogr., Sect. D: Biol. Crystallogr., 65, p. 41
Weiland, T. R., Kundu, S., Trent III, J. T., Hoy, J. A., Hargrove, M. S., (2004) J. Am. Chem. Soc., 126, p. 11930
Rifkind, J. M., Abugo, O., Levy, A., Heim, J. M., (1994) Methods Enzymol., 231, p. 449
Robinson, V. L., Smith, B. B., Arnone, A., (2003) Biochemistry, 42, p. 10113
Rachmilewitz, E. A., Peisach, J., Blumberg, W. E., (1971) J. Biol. Chem., 246, p. 3356
Trent III, J. T., Kundu, S., Hoy, J. A., Hargrove, M. S., (2004) J. Mol. Biol., 341, p. 1097
Mitchell, D. T., Kitto, G. B., Hackert, M. L., (1995) J. Mol. Biol., 251, p. 421
Sheldrick, G. M., (2008) Acta Crystallogr., Sect. D: Biol. Crystallogr., 64, p. 112
Jones, T. A., Kjeldgaard, M., (1988) Essential O, Software Manual, , Uppsala, p. 178
Jenkins, J. D., Musayev, F. N., Danso-Danquah, R., Abraham, D. J., Safo, M. K., (2009) Acta Crystallogr., Sect. D: Biol. Crystallogr., 65, p. 41
Rsc Adv (ISSN: 2046-2069), 2014; 4(49): 25852-25856.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.84, 5-year impact factor: 3.907
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84902981233&partnerID=40&md5=b1893d2203b1f9f47a4151ee0d690c58
Keywords: Cyanidation, Haemoglobins, Structural Modifications, Tetrameric, X Ray Crystal Structures,
Affiliations:
*** IBB - CNR ***
Dept of Chemical Sciences, University of Naples Federico II, Naples, Italy
Institute of Biostructures and Bioimaging, CNR, Naples, Italy
Institute of Biosciences and BioResources, CNR, Naples, Italy
Roma 3 University, Dept of Biology, Rome, Italy
Dept of Biophysics and Physiology, Albert Einstein College of Medicine, New York NY, United States
References:
Kakar, S., Hoffman, F.G., Storz, J.F., Fabian, M., Hargrove, M.S., (2010) Biophys. Chem., 152, p.
Merlino, A., Howes, B., Verde, C., Di Prisco, G., Smulevich, G., Mazzarella, L., Vergara, A., (2011) IUBMB Life, 63, p. 295
Wittenberg, J., Wittenberg, B., Gibson, Q., Trinick, M., Appleby, C., (1986) J. Biol. Chem., 261, p. 13624
Weiland, T.R., Kundu, S., Trent III, J.T., Hoy, J.A., Hargrove, M.S., (2004) J. Am. Chem. Soc., 126, p. 11930
Rifkind, J.M., Abugo, O., Levy, A., Heim, J.M., (1994) Methods Enzymol., 231, p. 449
Pesce, A., De Sanctis, D., Nardini, M., Dewilde, S., Moens, L., Hankeln, T., Burmester, T., Bolognesi, M., (2004) IUBMB Life, 56, p. 657
Tokumasu, F., Nardone, G.A., Ostera, G.R., Fairhurst, R.M., Beaudry, S.D., Hayakawa, E., Dvorak, J.A., (2009) PLoS One, 4, p. 1
Vergara, A., Franzese, M., Merlino, A., Bonomi, G., Verde, C., Giordano, D., Di Prisco, G., Mazzarella, L., (2009) Biophys. J., 97, p. 866
Robinson, V.L., Smith, B.B., Arnone, A., (2003) Biochemistry, 42, p. 10113
Ramesh, P., Sundaresan, S.S., Moorthy, P.S., Balasubramanian, M., Ponnnuswamy, M.N., (2013) J. Synchrotron Radiat., 20, p. 843
Ronda, L., Merlino, A., Bettati, S., Verde, C., Balsamo, A., Mazzarella, L., Mozzarelli, A., Vergara, A., (2013) Biochim. Biophys. Acta, Proteins Proteomics, 1834, p. 1885
Balsamo, A., Sannino, F., Merlino, A., Parrilli, E., Tutino, M.L., Mazzarella, L., Vergara, A., (2012) Biochimie, 94, p. 953
Rachmilewitz, E.A., Peisach, J., Blumberg, W.E., (1971) J. Biol. Chem., 246, p. 3356
Trent III, J.T., Kundu, S., Hoy, J.A., Hargrove, M.S., (2004) J. Mol. Biol., 341, p. 1097
De Sanctis, D., Ascenzi, P., Bocedi, A., Dewilde, S., Burmester, T., Hankeln, T., Moens, L., Bolognesi, M., (2006) Biochemistry, 45, p. 10054
Mitchell, D.T., Kitto, G.B., Hackert, M.L., (1995) J. Mol. Biol., 251, p. 421
Otwinowski, Z., Minor, W., (1997) Methods Enzymol., 276 (PART A), p. 307
Sheldrick, G.M., (2008) Acta Crystallogr., Sect. D: Biol. Crystallogr., 64, p. 112
Jones, T.A., Kjeldgaard, M., (1988) Essential O, Software Manual, , Uppsala, p. 178
Vergara, A., Vitagliano, L., Verde, C., Di Prisco, G., Mazzarella, L., (2008) Methods Enzymol., 436 (425), p. 56
Camardella, L., Caruso, C., D'Avino, R., Di Prisco, G., Rutigliano, B., Tamburrini, M., Fermi, G., Perutz, M.F., (1992) J. Mol. Biol., 224, p. 449
Verde, C., Vergara, A., Mazzarella, L., Di Prisco, G., (2008) Curr. Protein Pept. Sci., 9, p. 578
Vitagliano, L., Vergara, A., Bonomi, G., Merlino, A., Verde, C., Di Prisco, G., Howes, B.D., Mazzarella, L., (2008) J. Am. Chem. Soc., 130, p. 10527
Merlino, A., Vitagliano, L., Howes, B.D., Verde, C., Di Prisco, G., Smulevich, G., Sica, F., Vergara, A., (2009) Biopolymers, 91, p. 1117
Capece, L., Boechi, L., Perissinotti, L.L., Arroyo-Mañez, P., Bikiel, D.E., Smulevich, G., Marti, M.A., Estrin, D.A., (2013) Biochim. Biophys. Acta, 1834 (1722), p. 57
Jenkins, J.D., Musayev, F.N., Danso-Danquah, R., Abraham, D.J., Safo, M.K., (2009) Acta Crystallogr., Sect. D: Biol. Crystallogr., 65, p. 41
Weiland, T. R., Kundu, S., Trent III, J. T., Hoy, J. A., Hargrove, M. S., (2004) J. Am. Chem. Soc., 126, p. 11930
Rifkind, J. M., Abugo, O., Levy, A., Heim, J. M., (1994) Methods Enzymol., 231, p. 449
Robinson, V. L., Smith, B. B., Arnone, A., (2003) Biochemistry, 42, p. 10113
Rachmilewitz, E. A., Peisach, J., Blumberg, W. E., (1971) J. Biol. Chem., 246, p. 3356
Trent III, J. T., Kundu, S., Hoy, J. A., Hargrove, M. S., (2004) J. Mol. Biol., 341, p. 1097
Mitchell, D. T., Kitto, G. B., Hackert, M. L., (1995) J. Mol. Biol., 251, p. 421
Sheldrick, G. M., (2008) Acta Crystallogr., Sect. D: Biol. Crystallogr., 64, p. 112
Jones, T. A., Kjeldgaard, M., (1988) Essential O, Software Manual, , Uppsala, p. 178
Jenkins, J. D., Musayev, F. N., Danso-Danquah, R., Abraham, D. J., Safo, M. K., (2009) Acta Crystallogr., Sect. D: Biol. Crystallogr., 65, p. 41
Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin
Ferric cold-adapted fish haemoglobins exhibit heterogeneous coordination at the alpha (aquo-met) and beta (bis-histidyl) subunits. Herein we report two EPR-distinct bis-histidyl conformers (I and II) of the beta subunits of ferric haemoglobin from Trematomus bernacchii which react differently with CN-. An EPR titration reveals that upon cyanidation the most distorted conformer I reacts faster than II, producing both a cyanided and penta-coordinate ferric forms in the b subunits. The X-ray crystal structure of the partially cyanided conformer I reveals both an order-disorder transition and details of a communication between alpha and beta subunits.
Ferric cold-adapted fish haemoglobins exhibit heterogeneous coordination at the alpha (aquo-met) and beta (bis-histidyl) subunits. Herein we report two EPR-distinct bis-histidyl conformers (I and II) of the beta subunits of ferric haemoglobin from Trematomus bernacchii which react differently with CN-. An EPR titration reveals that upon cyanidation the most distorted conformer I reacts faster than II, producing both a cyanided and penta-coordinate ferric forms in the b subunits. The X-ray crystal structure of the partially cyanided conformer I reveals both an order-disorder transition and details of a communication between alpha and beta subunits.
Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin
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Structural modifications induced by the switch from an endogenous bis-histidyl to an exogenous cyanomet hexa-coordination in a tetrameric haemoglobin
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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
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View Export to BibTeX Export to EndNote
Vergara A, Franzese M, Merlino A, Bonomi G, Verde C, Giordano D, Di Prisco G, Lee HC, Peisach J, Mazzarella L
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View Export to BibTeX Export to EndNote
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Ponticelli S, Takeda A, Mitola S, Stassen J, Presta M, Ambati J, Ruvo M, De Falco S, Marasco D
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View Export to BibTeX Export to EndNote
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* Bis-histidyl Ferric Adducts in Tetrameric Haemoglobins (187 views)
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Vitagliano L, Vergara A, Bonomi G, Merlino A, Verde C, Di Prisco G, Howes BD, Smulevich G, Mazzarella L
* Spectroscopic And Crystallographic Characterization Of A Tetrameric Hemoglobin Oxidation Pathway Reveals Structural Features Of A Functional Intermediate R/T State (278 views)
Biophys J, 2008; 94: 4031-4040.
Impact Factor: 3.832
View Export to BibTeX Export to EndNote
Vergara A, Vitagliano L, Verde C, di Prisco G, Mazzarella L
* Spectroscopic and crystallographic characterization of bis-histidyl adducts in tetrameric hemoglobins (426 views)
Method Enzymol (ISSN: 0076-6879, 1557-7988electronic), 2008; 436: 425-444.
Impact Factor: 2.312
View Export to BibTeX Export to EndNote
Vergara A, Vitagliano L, Di Prisco G, Verde C, Mazzarella L
* Spectroscopic And Crystallographic Characterization Of Hemichromes In Tetrameric Hemoglobins (321 views)
Methods In Enzymology, 2008; 436: 421-440.
Impact Factor: 2.194
View Export to BibTeX Export to EndNote
Riccio A, Vitagliano L, Di Prisco G, Zagari A, Mazzarella L
* The crystal structure of a tetrameric hemoglobin in a partial hemichrome state (521 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2002 Jul 23; 99(15): 9801-9806.
Impact Factor: 10.7
View Export to BibTeX Export to EndNote
Riccio A, Vitagliano L, Di Prisco G, Zagari A, Mazzarella L
* Liganded and unliganded forms of Antarctic fish haemoglobins in polyethylene glycol: crystallization of an R-state haemichrome intermediate (392 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2001 Sep; 57: 1144-1146.
Impact Factor: 2.124
View Export to BibTeX Export to EndNote
14 Records (12 excluding Abstracts).
Total impact factor: 53.795 (52.141 excluding Abstracts).
Total 5 year impact factor: 62.049 (60.267 excluding Abstracts).
Total impact factor: 53.795 (52.141 excluding Abstracts).
Total 5 year impact factor: 62.049 (60.267 excluding Abstracts).
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