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Artículo

Cold-Adaptation Signatures in the Ligand Rebinding Kinetics to the Truncated Hemoglobin of the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125

Boubeta, Fernando MartínIcon ; Boechi, LeonardoIcon ; Estrin, Dario ArielIcon ; Patrizi, Barbara; Di Donato, Mariangela; Iagatti, Alessandro; Giordano, Daniela; Verde, Cinzia; Bruno, Stefano; Abbruzzetti, Stefania; Viappiani, Cristiano
Fecha de publicación: 12/2018
Editorial: American Chemical Society
Revista: Journal of Physical Chemistry B
ISSN: 1520-6106
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Físico-Química, Ciencia de los Polímeros, Electroquímica

Resumen

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.
Palabras clave: COLD ADAPTATION , LIGAND REBINDING KINETICS , P. HALOPLANKTIS , MOLECULAR DYNAMICS
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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/89445
URL: https://pubs.acs.org/doi/10.1021/acs.jpcb.8b07682
DOI: http://dx.doi.org/10.1021/acs.jpcb.8b07682
Colecciones
Articulos(OCA CIUDAD UNIVERSITARIA)
Articulos de OFICINA DE COORDINACION ADMINISTRATIVA CIUDAD UNIVERSITARIA
Articulos(INQUIMAE)
Articulos de INST.D/QUIM FIS D/L MATERIALES MEDIOAMB Y ENERGIA
Citación
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
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