Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins(485 views) Balsamo A, Sannino F, Merlino A, Parrilli E, Tutino ML, Mazzarella L, Vergara A
Keywords: β4 Hemoglobin, Bis-Histidyl Coordination, Expression, Molecular Dynamics, Hemoglobin Derivative, Iron, Tetramer, Beta Chain, Cloning, Human, Nonhuman, Protein Quaternary Structure, Protein Tertiary Structure, Purification, Review, Spectroscopy, Animals, Beta-Globins, Chromatography, Fish Proteins, Hemeproteins, Molecular Dynamics Simulation, Perciformes, Peroxidase, Protein Structure, Secondary, Protein Subunits, Recombinant Proteins, Trematomus Bernacchii,
Affiliations: *** IBB - CNR ***
Department of Chemistry, University of Naples Federico II, Via Cintia, I-80126 Naples, Italy
Department of Organic Chemistry and Biochemistry, University of Naples Federico II, 80126 Naples, Italy
Istituto di Biostrutture e Bioimmagini, CNR, 80134 Naples, Italy
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Rachmilewitz, E. A., Peisach, J., Blumberg, W. E., Studies on the stability of oxyhemoglobin A and its constituent chains and their derivatives (1971) J. Biol. Chem., 246, pp. 3356-3366
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Mitchell, D. T., Kitto, G. B., Hackert, M. L., Structural analysis of monomeric hemichrome and dimeric cyanomet hemoglobins from Caudina arenicola (1995) J. Mol. Biol., 251, pp. 421-431
Hargrove, M. S., Brucker, E. A., Stec, B., Sarath, G., Arredondo-Peter, R., Klucas, R. V., Olson, J. S., Phillips, Jr. G. N., Crystal structure of a nonsymbiotic plant hemoglobin (2000) Structure, 8, pp. 1005-1014
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Sorensen, H. P., Mortensen, K. K., Advanced genetic strategies for recombinant protein expression in Escherichia coli (2005) Journal of Biotechnology, 115 (2), pp. 113-128. , DOI 10. 1016/j. jbiotec. 2004. 08. 004, PII S0168165604004560
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Smith, D. M. A., Dupuis, M., Vorpagel, E. R., Straatsma, T. P., Characterization of electronic structure and properties of a bis (histidine) heme model complex (2003) Journal of the American Chemical Society, 125 (9), pp. 2711-2717. , DOI 10. 1021/ja0280473
Kerwin, B. A., Looker, D. G., Hess, E., Revilla-Sharp, P., Akers, M. J., Development of a storage stable liquid formulation for a recombinant hemoglobin (1997) Book of Abstracts, 213th ACS National Meeting, , San Francisco, April 13-17 I&EC-077
Hernan, R. A., Hui, H. L., Andracki, M. E., Noble, R. W., Sligar, S. G., Walder, J. A., Walder, R. Y., Human hemoglobin expression in Escherichia coli: Importance of optimal codon usage (1992) Biochemistry, 31, pp. 8619-8628
Borgstahl, G. E., Rogers, P. H., Arnone, A., The 1. 8 A structure of carbonmonoxy-beta 4 hemoglobin. Analysis of a homotetramer with the R quaternary structure of liganded alpha 2 beta 2 hemoglobin (1994) J. Mol. Biol., 236, pp. 817-830
Brooks III, C. L., Characterization of "native" apomyoglobin by molecular dynamics simulation (1992) J. Mol. Biol., 227, pp. 375-380
Yuk, Y. S., Ma, B., Tsai, C. -J., Nussinov, R., Molecular dynamics simulation of Escherichia coli dihydrofolate reductase and its protein fragments: Relative stabilities in experiment and simulations (2001) Protein Science, 10 (1), pp. 135-148. , DOI 10. 1110/ps. 33301
Doglia, S. M., Ami, D., Natalello, A., Gatti-Lafranconi, P., Lotti, M., Fourier transform infrared spectroscopy analysis of the conformational quality of recombinant proteins within inclusionbodies (2008) Biotechnology Journal, 3 (2), pp. 193-201. , DOI 10. 1002/biot. 200700238
Johnston, I. A., Muscle metabolism and growth in Antarctic fishes (suborder Notothenioidei): Evolution in a cold environment (2003) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 136 (4), pp. 701-713. , DOI 10. 1016/S1096-4959 (03) 00258-6
Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins
All tetrameric hemoglobins from Antarctic fish, including that from Trematomus bernacchii, HbTb form in the ferric state, promptly and distinctively from all the other tetrameric hemoglobins, a mixture of aquomet at the alpha subunits and bis-histidyl adduct (hemichrome) at the beta subunits. The role of the tertiary and quaternary structure in the hemichrome formation is unknown. Here we report the cloning, expression, purification, spectroscopic and computational characterization of the beta-chain of HUM (beta-HbTb). Similarly to the human beta-chains, beta-HbTb self-assembles to form the homotetramer beta-HbTb; however, the latter quantitatively forms reversible ferric and ferrous bis-histidyl adducts, which are only partially present in the human tetramer (beta(4)-HbA). A molecular dynamics study of the isolated beta subunit of the two Hbs indicates that the ability to form hemichrome is an intrinsic feature of the chain; moreover, the greater propensity of beta-HbTb to form the bis-histidyl adduct is probably linked to the higher flexibility of the CD loop region. On the bases of these experimental and computational results on the isolated chain, the influence of the quaternary structure on the stability of the endogenous ferrous and ferric hexa-coordination is also discussed. (C) 2011 Elsevier Masson SAS. All rights reserved.
Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins
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