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Referencias:

• Wittenberg, J.B., Bolognesi, M., Wittenberg, B.A., Guertin, M., Truncated hemoglobins: A new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants (2002) J. Biol. Chem., 277, pp. 871-874
• Wu, G., Wainwright, L.M., Poole, R.K., Microbial globins (2003) Adv. Microb. Physiol., 47, pp. 255-310
• Milani, M., Pesce, A., Nardini, M., Ouellet, H., Ouellet, Y., Dewilde, S., Bocedi, A., Bolognesi, M., Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins (2005) J. Inorg. Biochem., 99, pp. 97-109
• Vuletich, D.A., Lecomte, J.T., A phylogenetic and structural analysis of truncated hemoglobins (2006) J. Mol. Evol., 62, pp. 196-210
• Giangiacomo, L., Ilari, A., Boffi, A., Morea, V., Chiancone, E., The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties (2005) J. Biol. Chem., 280, pp. 9192-9202
• Bonamore, A., Ilari, A., Giangiacomo, L., Bellelli, A., Morea, V., Boffi, A., A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca (2005) FEBS J., 272, pp. 4189-4201
• Ilari, A., Kjelgaard, P., Von Wachenfeldt, C., Catacchio, B., Chiancone, E., Boffi, A., Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus (2007) Arch. Biochem. Biophys., 457, pp. 85-94
• Milani, M., Savard, P.Y., Ouellet, H., Ascenzi, P., Guertin, M., Bolognesi, M., A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O (2003) Proc. Natl. Acad. Sci. U.S.A., 100, pp. 5766-5771
• Ouellet, H., Juszczak, L., Dantsker, D., Samuni, U., Ouellet, Y.H., Savard, P.Y., Wittenberg, J.B., Guertin, M., Reactions of Mycobacterium tuberculosis truncated hemoglobin O with ligands reveal a novel ligand-inclusive hydrogen bond network (2003) Biochemistry, 42, pp. 5764-5774
• Boechi, L., Manez, P.A., Luque, F.J., Marti, M.A., Estrin, D.A., Unraveling the molecular basis for ligand binding in truncated hemoglobins: The trHbO Bacillus subtilis case (2010) Proteins, 78, pp. 962-970
• Feis, A., Lapini, A., Catacchio, B., Brogioni, S., Foggi, P., Chiancone, E., Boffi, A., Smulevich, G., Unusually strong H-bonding to the heme ligand and fast geminate recombination dynamics of the carbon monoxide complex of Bacillus subtilis truncated hemoglobin (2008) Biochemistry, 47, pp. 902-910
• Lu, C., Egawa, T., Mukai, M., Poole, R.K., Yeh, S.R., Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni: A comparative study with resonance Raman spectroscopy (2008) Methods Enzymol., 437, pp. 255-286
• Spiro, T.G., Wasbotten, I.H., CO as a vibrational probe of heme protein active sites (2005) J. Inorg. Biochem., 99, pp. 34-44
• Arroyo-Manez, P., Bikiel, D.E., Boechi, L., Capece, L., Di Lella, S., Estrin, D.A., Marti, M.A., Petruk, A.A., Protein dynamics and ligand migration interplay as studied by computer simulation (2010) Biochim. Biophys. Acta, , (in press)
• Bidon-Chanal, A., Marti, M.A., Estrin, D.A., Luque, F.J., Dynamical regulation of ligand migration by a gate-opening molecular switch in truncated hemoglobin-N from Mycobacterium tuberculosis (2007) J. Am. Chem. Soc., 129, pp. 6782-6788
• Boechi, L., Marti, 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, 73, pp. 372-379
• Marti, M.A., Bikiel, D.E., Crespo, A., Nardini, M., Bolognesi, M., Estrin, D.A., Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity (2006) Proteins, 62, pp. 641-648
• Marti, M.A., Capece, L., Bikiel, D.E., Falcone, B., Estrin, D.A., Oxygen affinity controlled by dynamical distal conformations: The soybean leghemoglobin and the Paramecium caudatum hemoglobin cases (2007) Proteins, 68, pp. 480-487
• Nicoletti, F.P., Comandini, A., Bonamore, A., Boechi, L., Boubeta, F.M., Feis, A., Smulevich, G., Boffi, A., Sulfide Binding Properties of Truncated Hemoglobins (2010) Biochemistry, 49, pp. 2269-2278
• Jorgensen, W.L., Chandrasekar, J., Madura, J., Impey, R.W., Klein, M.L., Comparison of simple potential functions for simulating liquid water (1983) J. Chem. Phys., 79, pp. 926-935
• Ryckaert, J.P., Ciccoti, G., Berendsen, H.J.C., Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes (1977) J. Comput. Phys., 23, pp. 327-341
• Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham, 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) Comput. Phys. Commun., 91, pp. 1-41
• Hori, H., Kitagawa, T., Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobin (1980) J. Am. Chem. Soc., 102, pp. 3608-3613
• Spiro, T.G., Li, X.-Y., Spiro, T.G., (1988) Biological Application of Raman Spectroscopy, 3, pp. 1-37. , in (Ed.) Vol., pp, Wiley-Interscience, New York
• Stein, P., Spiro, T.G., Hydrogen-bond and deprotonation effects on the resonance Raman iron-imidazole mode in deoxy hemoglobin models: Implication for hemoglobin cooperativity (1980) J. Am. Chem. Soc., 102, pp. 7795-7797
• Blackwood, Jr.M.E., Rush III, T.S., Romesberg, F., Schultz, P.G., Spiro, T.G., Alternative modes of substrate distortion in enzyme and antibody catalyzed ferrochelation reactions (1998) Biochemistry, 37, pp. 779-782
• Hu, S., Smith, K.M., Spiro, T.G., Assignment of Protoheme Resonance Raman Spectrum by Heme Labeling in Myoglobin (1996) J. Am. Chem. Soc., 118, pp. 12638-12646
• Smulevich, G., Hu, S.Z., Rodgers, K.R., Goodin, D.B., Smith, K.M., Spiro, T.G., Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes (1996) Biospectroscopy, 2, pp. 365-376
• Egawa, T., Yeh, S.R., Structural and functional properties of hemoglobins from unicellular organisms as revealed by resonance Raman spectroscopy (2005) J. Inorg. Biochem., 99, pp. 72-96
• Samuni, U., Ouellet, Y., Guertin, M., Friedman, J.M., Yeh, S.R., The absence of proximal strain in the truncated hemoglobins from Mycobacterium tuberculosis (2004) J. Am. Chem. Soc., 126, pp. 2682-2683
• Rwere, F., Mak, P.J., Kincaid, J.R., Resonance Raman interrogation of the consequences of heme rotational disorder in myoglobin and its ligated derivatives (2008) Biochemistry, 47, pp. 12869-12877
• Mie, Y., Yamada, C., Hareau, G.P., Neya, S., Uno, T., Funasaki, N., Nishiyama, K., Taniguchi, I., Functional evaluation of heme vinyl groups in myoglobin with symmetric protoheme isomers (2004) Biochemistry, 43, pp. 13149-13155
• Arcovito, A., Bonamore, A., Hazemann, J.L., Boffi, A., D'Angelo, P., Unusual proximal heme pocket geometry in the deoxygenated Thermobifida fusca: A combined spectroscopic investigation (2010) Biophys. Chem., 147, pp. 1-7
• Smulevich, G., Feis, A., Howes, B.D., Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: What have we learned? (2005) Acc. Chem. Res., 38, pp. 433-440
• Phillips, Jr.G.N., Teodoro, M.L., Li, T., Smith, B., Olson, J.S., Bound CO Is a Molecular Probe of Electrostatic Potential in the Distal Pocket of Myoglobin (1999) J. Phys. Chem. B, 103, pp. 8817-8829
• Cameron, A.D., Smerdon, S.J., Wilkinson, A.J., Habash, J., Helliwell, J.R., Li, T., Olson, J.S., Distal pocket polarity in ligand binding to myoglobin: Deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by X-ray crystallography and infrared spectroscopy (1993) Biochemistry, 32, pp. 13061-13070
• Mukai, M., Savard, P.Y., Ouellet, H., Guertin, M., Yeh, S.R., Unique ligand-protein interactions in a new truncated hemoglobin from Mycobacterium tuberculosis (2002) Biochemistry, 41, pp. 3897-3905
• Guallar, V., Lu, C., Borrelli, K., Egawa, T., Yeh, S.R., Ligand Migration in the Truncated Hemoglobin-II from Mycobacterium tuberculosis: The Role of G8 Tryptophan (2009) J. Biol. Chem., 284, pp. 3106-3116
• Ouellet, H., Milani, M., Labarre, M., Bolognesi, M., Couture, M., Guertin, M., The roles of Tyr(CD1) and Trp(G8) in Mycobacterium tuberculosis truncated hemoglobin O in ligand binding and on the heme distal site architecture (2007) Biochemistry, 46, pp. 11440-11450
• Milani, M., Ouellet, Y., Ouellet, H., Guertin, M., Boffi, A., Antonini, G., Bocedi, A., Ascenzi, P., Cyanide binding to truncated hemoglobins: A crystallographic and kinetic study (2004) Biochemistry, 43, pp. 5213-5221
• Feis, A., Santoni, E., Neri, F., Ciaccio, C., De Sanctis, G., Coletta, M., Welinder, K.G., Smulevich, G., Fine-tuning of the binding and dissociation of CO by the amino acids of the heme pocket of Coprinus cinereus peroxidase (2002) Biochemistry, 41, pp. 13264-13273
• Feis, A., Rodriguez-Lopez, J.N., Thorneley, R.N., Smulevich, G., The distal cavity structure of carbonyl horseradish peroxidase as probed by the resonance Raman spectra of His 42 Leu and Arg 38 Leu mutants (1998) Biochemistry, 37, pp. 13575-13581
• Uno, T., Nishimura, Y., Tsuboi, M., Makino, R., Iizuka, T., Ishimura, Y., Two types of conformers with distinct Fe-C-O configuration in the ferrous CO complex of horseradish peroxidase. Resonance Raman and infarared spectroscopic studies with native and deuteroheme-substituted enzymes (1987) J. Biol. Chem., 262, pp. 4549-4556
• Smulevich, G., Evangelista-Kirkup, R., English, A., Spiro, T.G., Raman and infrared spectra of cytochrome c peroxidase-carbon monoxide adducts in alternative conformational states (1986) Biochemistry, 25, pp. 4426-4430
• Torge, R., Comandini, A., Catacchio, B., Bonamore, A., Botta, B., Boffi, A., Peroxidase-like activity of Thermobifida fusca hemoglobin: The oxidation of dibenzylbutanolide (2009) J. Mol. Catal. B: Enzym., 61, pp. 303-308
• Ouellet, H., Ranguelova, K., Labarre, M., Wittenberg, J.B., Wittenberg, B.A., Magliozzo, R.S., Guertin, M., Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: Evidence for peroxidatic activity and formation of protein-based radicals (2007) J. Biol. Chem., 282, pp. 7491-7503

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