An Order-Disorder Transition Plays a Role in Switching Off the Root Effect in Fish Hemoglobins (535 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2010 Oct 15; 285(42): 32568-32575.
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Paper type: Journal Article,
Impact factor: 5.328, 5-year impact factor: 5.498
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77957778513&partnerID=40&md5=1916f0ba431e5e17b645d189c2b80ae2
Keywords: Crystal State, Electron Densities, Heme Iron, In-Line, Micro Spectroscopy, Root Effect, Side Chains, Spectroscopic Characterization, Structural Basis, Tetramers, Crystal Structure, Fish, Porphyrins, Hemoglobin, Aspartic Acid, Histidine, Alpha Chain, Controlled Study, Hydrogen Bond, Nonhuman, Priority Journal, Protein Stability, Protein Structure, Raman Spectrometry, Animals, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Quaternary, Tertiary, Spectrum Analysis, Trematomus Newnesi,
Affiliations:
*** IBB - CNR ***
Department of Chemistry, University of Naples Federico II, Naples I-80126, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Naples I-80134, Italy
Institute of Protein Biochemistry, CNR, Naples I-80131, Italy
References:
Not available.
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2010 Oct 15; 285(42): 32568-32575.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.328, 5-year impact factor: 5.498
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77957778513&partnerID=40&md5=1916f0ba431e5e17b645d189c2b80ae2
Keywords: Crystal State, Electron Densities, Heme Iron, In-Line, Micro Spectroscopy, Root Effect, Side Chains, Spectroscopic Characterization, Structural Basis, Tetramers, Crystal Structure, Fish, Porphyrins, Hemoglobin, Aspartic Acid, Histidine, Alpha Chain, Controlled Study, Hydrogen Bond, Nonhuman, Priority Journal, Protein Stability, Protein Structure, Raman Spectrometry, Animals, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Quaternary, Tertiary, Spectrum Analysis, Trematomus Newnesi,
Affiliations:
*** IBB - CNR ***
Department of Chemistry, University of Naples Federico II, Naples I-80126, Italy
Istituto di Biostrutture e Bioimmagini, CNR, Naples I-80134, Italy
Institute of Protein Biochemistry, CNR, Naples I-80131, Italy
References:
Not available.
An Order-Disorder Transition Plays a Role in Switching Off the Root Effect in Fish Hemoglobins
The Root effect is a widespread property among fish hemoglobins whose structural basis remains largely obscure. Here we report a crystallographic and spectroscopic characterization of the non-Root-effect hemoglobin isolated from the Antarctic fish Trematomus newnesi in the deoxygenated form. The crystal structure unveils that the T state of this hemoglobin is stabilized by a strong H-bond between the side chains of Asp95 alpha and Asp101 beta at the alpha(1)beta(2) and alpha(2)beta(1) interfaces. This unexpected finding undermines the accepted paradigm that correlates the presence of this unusual H-bond with the occurrence of the Root effect. Surprisingly, the T state is characterized by an atypical flexibility of two alpha chains within the tetramer. Indeed, regions such as the CD alpha corner and the EF alpha pocket, which are normally well ordered in the T state of tetrameric hemoglobins, display high B-factors and non-continuous electron densities. This flexibility also leads to unusual distances between the heme iron and the proximal and distal His residues. These observations are in line with Raman micro-spectroscopy studies carried out both in solution and in the crystal state. The findings here presented suggest that in fish hemoglobins the Root effect may be switched off through a significant destabilization of the T state regardless of the presence of the inter-aspartic H-bond. Similar mechanisms may also operate for other non-Root effect hemoglobins. The implications of the flexibility of the CD alpha corner for the mechanism of the T-R transition in tetrameric hemoglobins are also discussed.
The Root effect is a widespread property among fish hemoglobins whose structural basis remains largely obscure. Here we report a crystallographic and spectroscopic characterization of the non-Root-effect hemoglobin isolated from the Antarctic fish Trematomus newnesi in the deoxygenated form. The crystal structure unveils that the T state of this hemoglobin is stabilized by a strong H-bond between the side chains of Asp95 alpha and Asp101 beta at the alpha(1)beta(2) and alpha(2)beta(1) interfaces. This unexpected finding undermines the accepted paradigm that correlates the presence of this unusual H-bond with the occurrence of the Root effect. Surprisingly, the T state is characterized by an atypical flexibility of two alpha chains within the tetramer. Indeed, regions such as the CD alpha corner and the EF alpha pocket, which are normally well ordered in the T state of tetrameric hemoglobins, display high B-factors and non-continuous electron densities. This flexibility also leads to unusual distances between the heme iron and the proximal and distal His residues. These observations are in line with Raman micro-spectroscopy studies carried out both in solution and in the crystal state. The findings here presented suggest that in fish hemoglobins the Root effect may be switched off through a significant destabilization of the T state regardless of the presence of the inter-aspartic H-bond. Similar mechanisms may also operate for other non-Root effect hemoglobins. The implications of the flexibility of the CD alpha corner for the mechanism of the T-R transition in tetrameric hemoglobins are also discussed.
An Order-Disorder Transition Plays a Role in Switching Off the Root Effect in Fish Hemoglobins
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An Order-Disorder Transition Plays a Role in Switching Off the Root Effect in Fish Hemoglobins
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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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Protein titration in the crystal state (638 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Oct 1; 292(4): 845-854.
Impact Factor: 5.501
View Export to BibTeX Export to EndNote
Mazzarella L, D'Avino R, Di Prisco G, Savino C, Vitagliano L, Moody P, Zagari A
Crystal structure of Trematomus newnesi haemoglobin re-opens the Root effect question (614 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Apr 16; 287(5): 897-906.
Impact Factor: 5.501
View Export to BibTeX Export to EndNote
20 Records (20 excluding Abstracts).
Total impact factor: 102.103 (102.103 excluding Abstracts).
Total 5 year impact factor: 105.137 (105.137 excluding Abstracts).
Total impact factor: 102.103 (102.103 excluding Abstracts).
Total 5 year impact factor: 105.137 (105.137 excluding Abstracts).
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