Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state (942 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10527-10535.
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Paper type: Journal Article,
Impact factor: 8.091, 5-year impact factor: 8.256
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-49449107745&partnerID=40&md5=a4da15250f03fc8115ea5c72ed99fd0f
Keywords: Atomic Spectroscopy, Carbon Monoxide, Chemical Oxygen Demand, Iron, Leakage (fluid), Ligands, Nonmetals, Oxidation, Porphyrins, Allosteric Transition, Atomic Resolutions, Basic Concepts, Co Molecule, Crystallographic Characterization, Heme Iron, Intermediate Species, Oxidation Processes, Oxidation States, Oxidized States, Oxygen Release, Penta-Coordinated, Quaternary Structures, Spectroscopic Characterizations, Stereochemical Models, Structural Features, Structural Informations, Temporal Sequencing, Tertiary Structures, Hemoglobin, Iron Binding Protein, Tetramer, Alpha Chain, Antarctica, Article, Autooxidation, Beta Chain, Crystal Structure, Fish, Hemoglobin Determination, Phase Transition, Protein Binding, Protein Quaternary Structure, Protein Tertiary Structure, Stereochemistry, Structure Analysis, Animals, X-Ray, Fish Proteins, Oxidation-Reduction, Oxyhemoglobins, Perciformes, Protein Structure, Secondary, Spectrum Analysis,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Naples, Italy
Department of Chemistry, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, I-80126 Naples, Italy
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy
References:
Not available.
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10527-10535.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 8.091, 5-year impact factor: 8.256
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-49449107745&partnerID=40&md5=a4da15250f03fc8115ea5c72ed99fd0f
Keywords: Atomic Spectroscopy, Carbon Monoxide, Chemical Oxygen Demand, Iron, Leakage (fluid), Ligands, Nonmetals, Oxidation, Porphyrins, Allosteric Transition, Atomic Resolutions, Basic Concepts, Co Molecule, Crystallographic Characterization, Heme Iron, Intermediate Species, Oxidation Processes, Oxidation States, Oxidized States, Oxygen Release, Penta-Coordinated, Quaternary Structures, Spectroscopic Characterizations, Stereochemical Models, Structural Features, Structural Informations, Temporal Sequencing, Tertiary Structures, Hemoglobin, Iron Binding Protein, Tetramer, Alpha Chain, Antarctica, Article, Autooxidation, Beta Chain, Crystal Structure, Fish, Hemoglobin Determination, Phase Transition, Protein Binding, Protein Quaternary Structure, Protein Tertiary Structure, Stereochemistry, Structure Analysis, Animals, X-Ray, Fish Proteins, Oxidation-Reduction, Oxyhemoglobins, Perciformes, Protein Structure, Secondary, Spectrum Analysis,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, I-80134 Naples, Italy
Department of Chemistry, University of Naples Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, I-80126 Naples, Italy
Institute of Protein Biochemistry, CNR, Via Pietro Castellino 111, I-80131 Naples, Italy
References:
Not available.
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state
Tetrameric hemoglobins represent the most commonly used model for the description of the basic concepts of protein allostery. The classical stereochemical model assumes a concerted transition of the protein, upon oxygen release, from the relaxed (R) to the tense (T) state. Despite the large amount of data accumulated on the end-points of the transition, scarce structural information is available on the intermediate species along the pathway. Here we report a spectroscopic characterization of the autoxidation process of the Trematomus newnesi major Hb component and the atomic resolution structure (1.25 angstrom) of an intermediate form along the pathway characterized by a different binding and oxidation state of the a and beta chains. In contrast to the alpha-heme iron, which binds a CO molecule, the beta iron displays a pentacoordinated oxidized state, which is rare in tetrameric hemoglobins. Interestingly, the information provided by the present analysis is not limited to the characterization of the peculiar oxidation process of Antarctic fish hemoglobins. Indeed, this structure represents the most detailed snapshot of hemoglobin allosteric transition hitherto achieved. Upon ligand release at the beta heme, a cascade of structural events is observed. Notably, several structural features of the tertiary structure of the alpha and beta chains closely resemble those typically observed in the deoxygenated state. The overall quaternary structure also becomes intermediate between the R and the T state. The analysis of the alterations induced by the ligand release provides a clear picture of the temporal sequence of the events associated with the transition. The implications of the present findings have also been discussed in the wider context of tetrameric Hbs.
Tetrameric hemoglobins represent the most commonly used model for the description of the basic concepts of protein allostery. The classical stereochemical model assumes a concerted transition of the protein, upon oxygen release, from the relaxed (R) to the tense (T) state. Despite the large amount of data accumulated on the end-points of the transition, scarce structural information is available on the intermediate species along the pathway. Here we report a spectroscopic characterization of the autoxidation process of the Trematomus newnesi major Hb component and the atomic resolution structure (1.25 angstrom) of an intermediate form along the pathway characterized by a different binding and oxidation state of the a and beta chains. In contrast to the alpha-heme iron, which binds a CO molecule, the beta iron displays a pentacoordinated oxidized state, which is rare in tetrameric hemoglobins. Interestingly, the information provided by the present analysis is not limited to the characterization of the peculiar oxidation process of Antarctic fish hemoglobins. Indeed, this structure represents the most detailed snapshot of hemoglobin allosteric transition hitherto achieved. Upon ligand release at the beta heme, a cascade of structural events is observed. Notably, several structural features of the tertiary structure of the alpha and beta chains closely resemble those typically observed in the deoxygenated state. The overall quaternary structure also becomes intermediate between the R and the T state. The analysis of the alterations induced by the ligand release provides a clear picture of the temporal sequence of the events associated with the transition. The implications of the present findings have also been discussed in the wider context of tetrameric Hbs.
Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state
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Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state
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Impact Factor: 10.677
View Export to BibTeX Export to EndNote
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* Combined Crystallographic and Spectroscopic Analysis of Trematomus bernacchii Hemoglobin Highlights Analogies and Differences in the Peculiar Oxidation Pathway of Antarctic Fish Hemoglobins (715 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1117-1125.
Impact Factor: 2.605
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Randazzo R, Lauceri R, Mammana A, D'Urso A, Purrello R
* Interactions of Λ and Δ enantiomers of ruthenium(II) cationic complexes with achiral anionic porphyrins (696 views)
Chirality (ISSN: 0899-0042), 2009; 21(1): 92-96.
Impact Factor: 2.677
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Lauceri R, Fasciglione G, D'Urso A, Marini S, Purrello R, Coletta M
* Kinetic investigation of porphyrin interaction with chiral templates reveals unexpected features of the induction and self-propagation mechanism of chiral memory (847 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2008 Sep 13; 130(32): 10476-10477.
Impact Factor: 8.091
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Randazzo R, Mammana A, D'Urso A, Lauceri R, Purrello R
* Reversible "chiral memory" in ruthenium tris(phenanthroline)- anionic porphyrin complexes (771 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2008; 47(51): 9879-9882.
Impact Factor: 10.879
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Castiglioni E, Abbate S, Longhi G, Gangemi R, Lauceri R, Purrello R
* Absorption flattening as one cause of distortion of circular dichroism spectra of Δ-RuPhen3·H2TPPS complex (590 views)
Chirality (ISSN: 0899-0042), 2007 Sep; 19(8): 642-646.
Impact Factor: 2.436
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Matassa R, Carbone M, Lauceri R, Purrello R, Caminiti R
* Supramolecular structure of extrinsically chiral porphyrin hetero-assemblies and achiral analogues (753 views)
Adv Mater (ISSN: 0935-9648), 2007; 19(22): 3961-3967.
Impact Factor: 8.191
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Angela M, Massimo De N, Rosaria L, Roberto P
* Induction and memory of chirality in porphyrin hetero-aggregates: The role of the central metal ion (704 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 1464-3391electronic), 2005 Sep 1; 13(17): 5159-5163.
Impact Factor: 2.286
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Lauceria R, Purrellob R
* Transfer, memory and amplification of chirality in porphyrin aggregates (781 views)
Supramol Chem (ISSN: 1061-0278), 2005; 17(1-2): 61-66.
Impact Factor: 1.715
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Di Costanzo L, Geremia S, Randaccio L, Nastri F, Maglio O, Lombardi A, Pavone V
* Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV (901 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2004 Dec; 9(8): 1017-1027.
Impact Factor: 3.3
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Clemente F, D'Avino E, Guaragno M, Menichetti A
* An on line technique to detect cardiac output variations and cardiovascular performances during abdominal aortic surgery (934 views)
Journal Of Clinical Monitoring And Computing (ISSN: 1387-1307), 2004 Apr; 18(2): 81-87.
Impact Factor: 0.888
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Moschetto A, Lauceri R, Gulino FG, Sciotto D, Purrello R
* Non-covalent synthesis in aqueous solution of discrete multi-porphyrin aggregates with programmable stoichiometry and sequence (1318 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2002 Dec 11; 124(49): 14536-14537.
Impact Factor: 6.201
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Lauceri R, Raudino A, Scolaro LM, Micali N, Purrello R
* From achiral porphyrins to template-imprinted chiral aggregates and further. Self-replication of chiral memory from scratch (1854 views)
J Am Chem Soc (ISSN: 0002-7863print, 0002-7863linking, 1520-5126electronic), 2002 Feb 13; 120(47): 894-895.
Impact Factor: 9.023
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Lauceri R, Purrello R, Shetty SJ, Vicente MGH
* Interactions of anionic carboranylated porphyrins with DNA [3] (769 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2001 Jun 20; 123(24): 5835-5836.
Impact Factor: 6.079
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Aime S, Dastrù W, Gobetto R, Viale A
An NMR study of H(μ-H)Os3(CO)11 (624 views)
Inorg Chem (ISSN: 0020-1669, 1520-510x, 1520-510xelectronic), 2000; 39(11): 2422-2425.
Impact Factor: 2.712
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De Luca S, Bruno G, Fattorusso R, Isernia C, Pedone C, Morelli G
New synthetic tools for peptide-tetraphenylporphyrin derivatives (800 views)
Int J Pept Res Ther (ISSN: 0929-5666, 1573-3149), 1998 Jul; 5(4): 269-276.
Impact Factor: 0.557
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Nastri F, Lombardi A, D'Andrea LD, Sanseverino M, Maglio O, Pavone V
Miniaturized hemoproteins (798 views)
Biopolymers (ISSN: 0006-3525print, 0006-3525linking, 1097-0282electronic), 1998; 47(1): 5-22.
Impact Factor: 2.086
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Array
New Substituted Tetraphenyl Porphyrins: Synthesis, NMR Characterization and Manganese(II) and Iron(III) Complexes (156 views)
Journal Of Chemical Research Part S, 1998; (1 ): 18-19.
Impact Factor:
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Purrello R, Bellacchio E, Gurrieri S, Lauceri R, Raudino A, Monsù Scolaro L, Santoro AM
Ph Modulation Of Porphyrins Self-Assembly Onto Polylisine (638 views)
Journal Of Physical Chemistry B, 1998; N/D: 8852-8857.
Impact Factor: 0
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Colasanti A, Kisslinger A, Kusch D, Liuzzi R, Mastrocinque M, Montforts FP, Quarto M, Riccio P, Roberti G, Villani F
In vitro photo-activation of newly synthesized chlorin derivatives with red-light-emitting diodes (847 views)
J Photochem Photobiol B (ISSN: 1011-1344print, 1011-1344linking), 1997 Mar; 38(1): 54-60.
Impact Factor: 1.381
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Mastruzzo L, Woisard A, Ma DD, Rizzarelli E, Favre A, Le Doan T
TARGETED PHOTOCHEMICAL MODIFICATION OF HIV-DERIVED OLIGORIBONUCLEOTIDES BY ANTISENSE OLIGODEOXYNUCLEOTIDES LINKED TO PORPHYRINS (482 views)
Photochem Photobiol (ISSN: 0031-8655), 1994 Oct; 60(4): 316-322.
Impact Factor: 2.426
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Bustamante C, Gurrieri S, Pasternack RF, Purrello R, Rizzarelli E
Interaction of water-soluble porphyrins with single- and double-stranded polyribonucleotides (629 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1994 Sep; 34(8): 1099-1104.
Impact Factor: 2.425
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36 Records (36 excluding Abstracts).
Total impact factor: 147.663 (147.663 excluding Abstracts).
Total 5 year impact factor: 163.342 (163.342 excluding Abstracts).
Total impact factor: 147.663 (147.663 excluding Abstracts).
Total 5 year impact factor: 163.342 (163.342 excluding Abstracts).
942 views. Last view on Tuesday 29 April 2025, 22:07:36
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