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dc.contributor.author
Boubeta, Fernando Martín  
dc.contributor.author
Boechi, Leonardo  
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Estrin, Dario Ariel  
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Patrizi, Barbara  
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Di Donato, Mariangela  
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Iagatti, Alessandro  
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Giordano, Daniela  
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Verde, Cinzia  
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Bruno, Stefano  
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Abbruzzetti, Stefania  
dc.contributor.author
Viappiani, Cristiano  
dc.date.available
2019-11-21T19:06:03Z  
dc.date.issued
2018-12  
dc.identifier.citation
Boubeta, Fernando Martín; Boechi, Leonardo; Estrin, Dario Ariel; Patrizi, Barbara; Di Donato, Mariangela; et al.; Cold-Adaptation Signatures in the Ligand Rebinding Kinetics to the Truncated Hemoglobin of the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125; American Chemical Society; Journal of Physical Chemistry B; 122; 49; 12-2018; 11649-11661  
dc.identifier.issn
1520-6106  
dc.identifier.uri
http://hdl.handle.net/11336/89445  
dc.description.abstract
Cold-adapted organisms have evolved proteins endowed with higher flexibility and lower stability in comparison to their thermophilic homologues, resulting in enhanced reaction rates at low temperatures. In this context, protein-bound water molecules were suggested to play a major role, and their weaker interactions at protein active sites have been associated with cold adaptation. In this work, we tested this hypothesis on truncated hemoglobins (a family of microbial heme-proteins of yet-unclear function) applying molecular dynamics simulations and ligand-rebinding kinetics on a protein from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 in comparison with its thermophilic Thermobifida fusca homologue. The CO rebinding kinetics of the former highlight several geminate phases, with an unusually long-lived geminate intermediate. An articulated tunnel with at least two distinct docking sites was identified by analysis of molecular dynamics simulations and was suggested to be at the origin of the unusual geminate rebinding phase. Water molecules are present in the distal pocket, but their stabilization by TrpG8, TyrB10, and HisCD1 is much weaker than in thermophilic Thermobifida fusca truncated hemoglobin, resulting in a faster geminate rebinding. Our results support the hypothesis that weaker water-molecule interactions at the reaction site are associated with cold adaptation.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
American Chemical Society  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
COLD ADAPTATION  
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LIGAND REBINDING KINETICS  
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P. HALOPLANKTIS  
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MOLECULAR DYNAMICS  
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica  
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Ciencias Químicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Cold-Adaptation Signatures in the Ligand Rebinding Kinetics to the Truncated Hemoglobin of the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
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info:eu-repo/semantics/publishedVersion  
dc.date.updated
2019-10-16T15:23:04Z  
dc.journal.volume
122  
dc.journal.number
49  
dc.journal.pagination
11649-11661  
dc.journal.pais
Estados Unidos  
dc.description.fil
Fil: Boubeta, Fernando Martín. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina  
dc.description.fil
Fil: Boechi, Leonardo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Cálculo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina  
dc.description.fil
Fil: Estrin, Dario Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de los Materiales, Medioambiente y Energía. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina  
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Fil: Patrizi, Barbara. Università di Firenze. Lens European Laboratory For Non-linear Spectroscopy; Italia. Istituto Nazionale di Ottica; Italia  
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Fil: Di Donato, Mariangela. Università di Firenze. Lens European Laboratory For Non-linear Spectroscopy; Italia. Istituto Nazionale di Ottica; Italia  
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Fil: Iagatti, Alessandro. Università di Firenze. Lens European Laboratory For Non-linear Spectroscopy; Italia  
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Fil: Giordano, Daniela. Consiglio Nazionale delle Ricerche; Italia. Stazione Zoologica Anton Dohrn; Italia  
dc.description.fil
Fil: Verde, Cinzia. Consiglio Nazionale delle Ricerche; Italia. Stazione Zoologica Anton Dohrn; Italia  
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Fil: Bruno, Stefano. Università di Parma; Italia  
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Fil: Abbruzzetti, Stefania. Università di Parma; Italia  
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Fil: Viappiani, Cristiano. Università di Parma; Italia  
dc.journal.title
Journal of Physical Chemistry B  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/acs.jpcb.8b07682  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1021/acs.jpcb.8b07682