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Referencias:

• Perutz, M.F., Fermi, G., Luisi, B., Shaanan, B., Liddington, R.C., Stereochemistry of cooperative mechanisms in hemoglobin (1987) Acc. Chem. Res., 9, pp. 309-321
• Yokoyama, T., Chong, K.T., Miyazaki, G., Morimoto, H., Shih, D.T.-B., Unzai, S., Tame, J.R.H., Park, S.-Y., Novel mechanisms of pH sensitivity in tuna hemoglobin. A structural explanation of the root effect (2004) Journal of Biological Chemistry, 279 (27), pp. 28632-28640. , DOI 10.1074/jbc.M401740200
• Brittain, T., The Root effect in hemoglobins (2005) J. Inorg. Biochem., 99, pp. 120-129
• Tame, J.R., Wilson, J.C., Weber, R.E., The crystal structures of trout Hb i in the deoxy and carbonmonoxy forms J. Mol. Biol., 259, pp. 749-760
• Mylvaganam, S.E., Bonaventura, C., Bonaventura, J., Getzoff, E.D., Structural basis for the root effect in haemoglobin (1996) Nature Structural Biology, 3 (3), pp. 275-283. , DOI 10.1038/nsb0396-275
• Berenbrink, M., Koldkjaer, P., Kepp, O., Cossins, A.R., Evolution of oxygen secretion in fishes and the emergence of a complex physiological system (2005) Science, 307 (5716), pp. 1752-1757. , DOI 10.1126/science.1107793
• Camardella, L., Caruso, C., D'Avino, R., Di Prisco, G., Rutigliano, B., Tamburini, M., Fermi, G., Perutz, M.F., Hemoglobin of the Antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative (1992) J. Mol. Biol., 224, pp. 449-460
• Ito, N., Komiyama, N.H., Fermi, G., Structure of deoxyhemoglobin of the Antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and unliganded hemoglobin structures (1995) J. Mol. Biol., 250, pp. 648-658
• Mazzarella, L., Vergara, A., Vitagliano, L., Merlino, A., Bonomi, G., Scala, S., Verde, C., Di Prisco, G., High resolution crystal structure of deoxy hemoglobin from Trematomus bernacchii at different pH values: The role of histidine residues in modulating the strength of the root effect (2006) Proteins: Structure, Function and Genetics, 65 (2), pp. 490-498. , DOI 10.1002/prot.21114
• Mazzarella, L., Bonomi, G., Lubrano, M.C., Merlino, A., Riccio, A., Vergara, A., Vitagliano, L., Di Prisco, G., Minimal structural requirements for root effect: Crystal structure of the cathodic hemoglobin isolated from the Antarctic fish Trematomus newnesi (2006) Proteins: Structure, Function and Genetics, 62 (2), pp. 316-321. , DOI 10.1002/prot.20709
• 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 (2010) J. Biol. Chem., 285, pp. 32568-32575
• Mazzarella, L., D'Avino, R., Di Prisco, G., Savino, C., Vitagliano, L., Moody, P.C.E., Zagari, A., Crystal structure of trematomus newnesi haemoglobin re-opens the root effect question (1999) Journal of Molecular Biology, 287 (5), pp. 897-906. , DOI 10.1006/jmbi.1999.2632
• Merlino, A., Verde, C., Di Prisco, G., Mazzarella, L., Vergara, A., Reduction of ferric hemoglobin from Trematomus bernacchii in a partial bis-histidyl state produces a deoxy coordination even when encapsulated into the crystal phase (2008) Spectroscopy, 22 (2-3), pp. 143-152. , DOI 10.3233/SPE-2008-0332, XII European Conference on the Spectroscopy of Biological Molecules, Bobigny, France, 1-6 September 2007, Part 1
• Merlino, A., Vitagliano, L., Howes, B., 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 (2009) Biopolymers, 91, pp. 1117-1125
• Vergara, A., Franzese, M., Merlino, A., Bonomi, G., Verde, C., Giordano, D., Di Prisco, G., Mazzarella, L., Correlation between hemichrome stability and the Root effect in tetrameric hemoglobins (2009) Biophys. J., 97, pp. 866-874
• Vergara, A., Franzese, M., Merlino, A., Vitagliano, L., Verde, C., Di Prisco, G., Lee, H.C., Mazzarella, L., Structural characterization of ferric hemoglobins from three Antarctic fish species of the suborder notothenioidei (2007) Biophysical Journal, 93 (8), pp. 2822-2829. , http://www.biophysj.org/cgi/reprint/93/8/2822, DOI 10.1529/biophysj.107.105700
• Vitagliano, L., Vergara, A., Bonomi, G., Merlino, A., Verde, C., Di Prisco, G., Howes, B.D., Mazzarella, L., Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state (2008) J. Am. Chem. Soc., 130, pp. 10527-10535
• Baldwin, J., Chothia, C., Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism (1979) Journal of Molecular Biology, 129 (2), pp. 175-220. , DOI 10.1016/0022-2836(79)90277-8
• Ackers, G.K., Deciphering the molecular code of hemoglobin allostery (1998) Advances in Protein Chemistry, 51, pp. 185-253
• 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 (2010) J. Phys. Chem. B, 114, pp. 7002-7008
• Scott, E.E., Gibson, Q.H., Olson, J.S., Distal histidine stabilizes bound O 2 and acts as a gate for ligand entry in both subunits of adult human hemoglobin (2010) J. Biol. Chem., 285, pp. 8840-8854
• Tilton, Jr.R.F., Kuntz, Jr.I.D., Petsko, G.A., Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 Å (1984) Biochemistry, 23, pp. 2849-2857
• Tilton, Jr.R.F., Singh, U.C., Kuntz, Jr.I.D., Kollman, P.A., Protein-ligand dynamics. A 96 picosecond simulation of a myoglobin-xenon complex (1988) J. Mol. Biol., 199, pp. 195-211
• Elber, R., Karplus, M., Enhanced sampling in molecular dynamics: Use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin (1990) J. Am. Chem. Soc., 112, pp. 9161-9175
• Boechi, L., Martí, M.A., Milani, M., Bolognesi, M., Luque, F.J., Estrin, D.A., Structural determinants of ligand migration in Mycobacterium tuberculosis truncated hemoglobin O (2008) Proteins Struct. Funct. Bioinf., 73, pp. 372-379
• Capece, L., Estrin, D.A., Marti, M.A., Dynamical characterization of the heme NO oxygen binding (HNOX) domain. Insight into soluble guanylate cyclase allosteric transition (2008) Biochemistry, 47, pp. 9416-9427
• Perissinotti, L.L., Marti, M.A., Doctorovich, F., Luque, F.J., Estrin, D.A., A microscopic study of the deoxyhemoglobin-catalyzed generation of nitric oxide from nitrite anion (2008) Biochemistry, 47, pp. 9793-9802
• Capece, L., Marti, M.A., Bidon-Chanal, A., Nadra, A., Luque, F.J., Estrin, D.A., High pressure reveals structural determinants for globin hexacoordination: Neuroglobin and myoglobin cases (2009) Proteins Struct. Funct. Bioinf., 75, pp. 885-894
• Martí, M.A., Estrin, D.A., Roitberg, A.E., Molecular basis for the pH dependent structural transition of Nitrophorin 4 (2009) J. Phys. Chem. B, 113, pp. 2135-2142
• Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham Iii, T.E., Debolt, S., Ferguson, D., Kollman, P., Amber, a Package of Computer-Programs for Applying Molecular Mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules (1995) Comp. Phys. Comm., 91, pp. 1-3. , 1-41
• Hornak, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A., Simmerling, C., Comparison of multiple amber force fields and development of improved protein backbone parameters (2006) Proteins: Structure, Function and Genetics, 65 (3), pp. 712-725. , DOI 10.1002/prot.21123
• Mongan, J., Case, D.A., McCammon, J.A., Constant pH molecular dynamics in generalized born implicit solvent (2004) J. Comput. Chem., 25, pp. 2038-2048
• Cohen, J., Olsen, K.W., Schulten, K., Finding gas migration pathways in proteins using implicit ligand sampling (2008) Methods Enzymol., 437, pp. 439-457
• Humphrey, W., Dalke, A., Schulten, K., VMD-visual molecular dynamics (1996) J. Mol. Graph., 14, pp. 33-38
• Lama, A., Pawaria, S., Bidon-Chanal, A., Anand, A., Gelpí, J.L., Arya, S., Martí, M., Dikshit, K.L., Role of Pre-A motif in nitric oxide scavenging by truncated hemoglobin, HbN, of Mycobacterium tuberculosis (2009) J. Biol. Chem., 284, pp. 14457-14468
• Guallar, V., Jarzecki, A.A., Friesner, R.A., Spiro, T.G., Modeling of ligation-induced helix/loop displacements in myoglobin: Toward an understanding of hemoglobin allostery (2006) J. Am. Chem. Soc., 128, pp. 5427-5435
• Alcantara, R.E., Xu, C., Spiro, T.G., Guallar, V., A quantum-chemical picture of hemoglobin affinity (2007) Proceedings of the National Academy of Sciences of the United States of America, 104 (47), pp. 18451-18455. , http://www.pnas.org/cgi/reprint/104/47/18451, DOI 10.1073/pnas.0706026104
• Perutz, M.F., Mechanisms of cooperativity and allosteric regulation in proteins (1989) Q. Rev. Biophys., 22, pp. 139-237
• Vallone, B., Nienhaus, K., Matthes, A., Brunori, M., Nienhaus, G.U., The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity (2004) Proceedings of the National Academy of Sciences of the United States of America, 101 (50), pp. 17351-17356. , DOI 10.1073/pnas.0407633101
• Jenkins, J.D., Mausayev, F.N., Danso-Danquah, R., Abraham, D.J., Safo, M.K., Structure of relaxed-state of human haemoglobin:insight into ligand uptake, transport and release (2009) Acta Cryst. D, 65, pp. 41-48
• Olson, J.S., Soman, J., Phillips Jr., G.N., Ligand pathways in myoglobin: A review of trp cavity mutations (2007) IUBMB Life, 59 (8-9), pp. 552-562. , DOI 10.1080/15216540701230495, PII 778491829, IUBMB Life Dedicated to Maurizio Brunori in the Occasion of his 70th Birthday
• Yang, F., Phillips Jr., G.N., Crystal structures of CO-, Deoxy- and Met-myoglobins at various pH values (1996) Journal of Molecular Biology, 256 (4), pp. 762-774. , DOI 10.1006/jmbi.1996.0123
• Scott, E.E., Gibson, Q.H., Olson, J.S., Mapping the pathway for O 2 entry into and exit from myoglobin (2001) J. Biol. Chem., 276, pp. 5177-5188

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