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dc.contributor.author
Nicoletti, Francesco P.
dc.contributor.author
Droghetti, Enrica
dc.contributor.author
Howes, Barry D.
dc.contributor.author
Bustamante, Juan Pablo
dc.contributor.author
Bonamore, Alessandra
dc.contributor.author
Sciamanna, Natascia
dc.contributor.author
Estrin, Dario Ariel
dc.contributor.author
Feis, Alessandro
dc.contributor.author
Boffi, Alberto
dc.contributor.author
Smulevich, Giulietta
dc.date.available
2016-11-03T21:48:59Z
dc.date.issued
2013-02
dc.identifier.citation
Nicoletti, Francesco P.; Droghetti, Enrica; Howes, Barry D.; Bustamante, Juan Pablo; Bonamore, Alessandra; et al.; H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1834; 9; 2-2013; 315-324
dc.identifier.issn
1570-9639
dc.identifier.uri
http://hdl.handle.net/11336/7971
dc.description.abstract
The ferric form of truncated hemoglobin II from Thermobifida fusca (Tf-trHb) and its triple mutant WG8F-YB10F-YCD1F at neutral and alkaline pH, and in the presence of CN− have been characterized by resonance Raman spectroscopy, electron paramagnetic resonance spectroscopy, and molecular dynamics simulations. Tf-trHb contains three polar residues in the distal site, namely TrpG8, TyrCD1 and TyrB10. Whereas TrpG8 can act as a potential hydrogen-bond donor, the tyrosines can act as donors or acceptors. Ligand binding in heme-containing proteins is determined by a number of factors, including the nature and conformation of the distal residues and their capability to stabilize the heme-bound ligand via hydrogen-bonding and electrostatic interactions. Since both the RR Fe-OH− and Fe-CN− frequencies are very sensitive to the distal environment, detailed information on structural variations has been obtained. The hydroxyl ligand binds only the WT protein giving rise to two different conformers. In form 1 the anion is stabilized by H-bonds with TrpG8, TyrCD1 and a water molecule, in turn H-bonded to TyrB10. In form 2, H-bonding with TyrCD1 is mediated by a water molecule. Unlike the OH− ligand, CN− binds both WT and the triple mutant giving rise to two forms with similar spectroscopic characteristics. The overall results clearly indicate that H-bonding interactions both with distal residues and water molecules are important structural determinants in the active site of Tf-trHb.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Resonance Raman
dc.subject
Molecular Dynamics Simulations
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Thermobifida Fusca Hemoglobin
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Hydroxyl Ligand
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Cyanide Ligand
dc.subject.classification
Físico-Química, Ciencia de los Polímeros, Electroquímica
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Ciencias Químicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2016-10-25T19:28:25Z
dc.journal.volume
1834
dc.journal.number
9
dc.journal.pagination
315-324
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Nicoletti, Francesco P.. Universita Degli Studi Di Firenze; Italia
dc.description.fil
Fil: Droghetti, Enrica. Universita Degli Studi Di Firenze; Italia
dc.description.fil
Fil: Howes, Barry D.. Universita Degli Studi Di Firenze; Italia
dc.description.fil
Fil: Bustamante, Juan Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química, Física de Los Materiales, Medioambiente y Energía; Argentina. Universidad de Buenos Aires; Argentina
dc.description.fil
Fil: Bonamore, Alessandra. Universita Di Roma; Italia
dc.description.fil
Fil: Sciamanna, Natascia. Universita Di Roma; Italia
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; Argentina. Universidad de Buenos Aires; Argentina
dc.description.fil
Fil: Feis, Alessandro. Universita Degli Studi Di Firenze; Italia
dc.description.fil
Fil: Boffi, Alberto. Universita Di Roma; Italia. Centro Nazionale di Ricerca. Institute Pasteur; Italia
dc.description.fil
Fil: Smulevich, Giulietta. Universita Degli Studi Di Firenze; Italia
dc.journal.title
Biochimica Et Biophysica Acta-proteins And Proteomics
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.doi.org/10.1016/j.bbapap.2013.02.033
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1570963913001040
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