Role of the tertiary and quaternary structure in the formation of bis-histidyl adducts in cold-adapted hemoglobins(587 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
References: Not available.
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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Santulli G, Cipolletta E, Sorriento D, Del Giudice C, Anastasio A, Monaco S, Maione AS, Condorelli G, Puca A, Trimarco B, Illario M, Iaccarino G * CaMK4 gene deletion induces hypertension(412 views) J Am Heart Assoc Journal Of The American Heart Association (ISSN: 2047-9980), 2012; 1(4): N/D-N/D. Impact Factor:2.882 ViewExport to BibTeXExport to EndNote
Testino G, Leone S, Fagoonee S, Del Bas JM, Rodriguez B, Puiggros F, Marine S, Rodriguez MA, Morina D, Armengol L, Caimari A, Arola L, Cimini FA, Barchetta I, Carotti S, Bertoccini L, Baroni MG, Vespasiani-gentilucci U, Cavallo MG, Morini S, Nelson JE, Roth CL, Wilson LA, Yates KP, Aouizerat B, Morgan-stevenson V, Whalen E, Hoofnagle A, Mason M, Gersuk V, Yeh MM, Kowdley KV, Lee SM, Jun DW, Cho YK, Jang KS, Kucukazman M, Ata N, Dal K, Yeniova AO, Kefeli A, Basyigit S, Aktas B, Akin KO, Agladioglu K, Ure OS, Topal F, Nazligul Y, Beyan E, Ertugrul DT, Catena C, Cosma C, Camozzi V, Plebani M, Ermani M, Sechi LA, Fallo F, Goto Y, Ray MB, Mendenhall CL, French SW, Gartside PS Serum vitamin A deficiency and increased intrahepatic expression of cytokeratin antigen in alcoholic liver disease(707 views) Hepatology (ISSN: 1827-1669electronic, 0026-4806linking), 1988 Sep; 83120693611123109(5): 1019-1026. Impact Factor:0.913 ViewExport to BibTeXExport to EndNote
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