http://purl.uniprot.org/citations/20610398 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/20610398 | http://www.w3.org/2000/01/rdf-schema#comment | "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 Asp95α and Asp101β at the α(1)β(2) and α(2)β(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 α chains within the tetramer. Indeed, regions such as the CDα corner and the EFα 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 CDα corner for the mechanism of the T-R transition in tetrameric hemoglobins are also discussed."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m110.143537"xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/author | "Mazzarella L."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/author | "Sica F."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/author | "Marino K."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/author | "Verde C."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/author | "Vitagliano L."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/author | "di Prisco G."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/author | "Merlino A."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/author | "Vergara A."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/pages | "32568-32575"xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/title | "An order-disorder transition plays a role in switching off the root effect in fish hemoglobins."xsd:string |
http://purl.uniprot.org/citations/20610398 | http://purl.uniprot.org/core/volume | "285"xsd:string |
http://purl.uniprot.org/citations/20610398 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20610398 |
http://purl.uniprot.org/citations/20610398 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20610398 |
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http://purl.uniprot.org/uniprot/P45720 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20610398 |
http://purl.uniprot.org/uniprot/P45718 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20610398 |