H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin
- Autores
- Nicoletti, Francesco P.; Droghetti, Enrica; Howes, Barry D.; Bustamante, Juan Pablo; Bonamore, Alessandra; Sciamanna, Natascia; Estrin, Dario Ariel; Feis, Alessandro; Boffi, Alberto; Smulevich, Giulietta
- Año de publicación
- 2013
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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.
Fil: Nicoletti, Francesco P.. Universita Degli Studi Di Firenze; Italia
Fil: Droghetti, Enrica. Universita Degli Studi Di Firenze; Italia
Fil: Howes, Barry D.. Universita Degli Studi Di Firenze; Italia
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
Fil: Bonamore, Alessandra. Universita Di Roma; Italia
Fil: Sciamanna, Natascia. Universita Di Roma; Italia
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
Fil: Feis, Alessandro. Universita Degli Studi Di Firenze; Italia
Fil: Boffi, Alberto. Universita Di Roma; Italia. Centro Nazionale di Ricerca. Institute Pasteur; Italia
Fil: Smulevich, Giulietta. Universita Degli Studi Di Firenze; Italia - Materia
-
Resonance Raman
Molecular Dynamics Simulations
Thermobifida Fusca Hemoglobin
Hydroxyl Ligand
Cyanide Ligand - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/7971
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CONICET Digital (CONICET) |
spelling |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobinNicoletti, Francesco P.Droghetti, EnricaHowes, Barry D.Bustamante, Juan PabloBonamore, AlessandraSciamanna, NatasciaEstrin, Dario ArielFeis, AlessandroBoffi, AlbertoSmulevich, GiuliettaResonance RamanMolecular Dynamics SimulationsThermobifida Fusca HemoglobinHydroxyl LigandCyanide Ligandhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The 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.Fil: Nicoletti, Francesco P.. Universita Degli Studi Di Firenze; ItaliaFil: Droghetti, Enrica. Universita Degli Studi Di Firenze; ItaliaFil: Howes, Barry D.. Universita Degli Studi Di Firenze; ItaliaFil: 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; ArgentinaFil: Bonamore, Alessandra. Universita Di Roma; ItaliaFil: Sciamanna, Natascia. Universita Di Roma; ItaliaFil: 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; ArgentinaFil: Feis, Alessandro. Universita Degli Studi Di Firenze; ItaliaFil: Boffi, Alberto. Universita Di Roma; Italia. Centro Nazionale di Ricerca. Institute Pasteur; ItaliaFil: Smulevich, Giulietta. Universita Degli Studi Di Firenze; ItaliaElsevier Science2013-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/7971Nicoletti, 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; 315-3241570-9639enginfo:eu-repo/semantics/altIdentifier/url/http://www.doi.org/10.1016/j.bbapap.2013.02.033info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1570963913001040info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:15:44Zoai:ri.conicet.gov.ar:11336/7971instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:15:44.932CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin |
title |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin |
spellingShingle |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin Nicoletti, Francesco P. Resonance Raman Molecular Dynamics Simulations Thermobifida Fusca Hemoglobin Hydroxyl Ligand Cyanide Ligand |
title_short |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin |
title_full |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin |
title_fullStr |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin |
title_full_unstemmed |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin |
title_sort |
H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin |
dc.creator.none.fl_str_mv |
Nicoletti, Francesco P. Droghetti, Enrica Howes, Barry D. Bustamante, Juan Pablo Bonamore, Alessandra Sciamanna, Natascia Estrin, Dario Ariel Feis, Alessandro Boffi, Alberto Smulevich, Giulietta |
author |
Nicoletti, Francesco P. |
author_facet |
Nicoletti, Francesco P. Droghetti, Enrica Howes, Barry D. Bustamante, Juan Pablo Bonamore, Alessandra Sciamanna, Natascia Estrin, Dario Ariel Feis, Alessandro Boffi, Alberto Smulevich, Giulietta |
author_role |
author |
author2 |
Droghetti, Enrica Howes, Barry D. Bustamante, Juan Pablo Bonamore, Alessandra Sciamanna, Natascia Estrin, Dario Ariel Feis, Alessandro Boffi, Alberto Smulevich, Giulietta |
author2_role |
author author author author author author author author author |
dc.subject.none.fl_str_mv |
Resonance Raman Molecular Dynamics Simulations Thermobifida Fusca Hemoglobin Hydroxyl Ligand Cyanide Ligand |
topic |
Resonance Raman Molecular Dynamics Simulations Thermobifida Fusca Hemoglobin Hydroxyl Ligand Cyanide Ligand |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
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. Fil: Nicoletti, Francesco P.. Universita Degli Studi Di Firenze; Italia Fil: Droghetti, Enrica. Universita Degli Studi Di Firenze; Italia Fil: Howes, Barry D.. Universita Degli Studi Di Firenze; Italia 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 Fil: Bonamore, Alessandra. Universita Di Roma; Italia Fil: Sciamanna, Natascia. Universita Di Roma; Italia 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 Fil: Feis, Alessandro. Universita Degli Studi Di Firenze; Italia Fil: Boffi, Alberto. Universita Di Roma; Italia. Centro Nazionale di Ricerca. Institute Pasteur; Italia Fil: Smulevich, Giulietta. Universita Degli Studi Di Firenze; Italia |
description |
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. |
publishDate |
2013 |
dc.date.none.fl_str_mv |
2013-02 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/7971 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 1570-9639 |
url |
http://hdl.handle.net/11336/7971 |
identifier_str_mv |
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 1570-9639 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.doi.org/10.1016/j.bbapap.2013.02.033 info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1570963913001040 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Elsevier Science |
publisher.none.fl_str_mv |
Elsevier Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614095788048384 |
score |
13.070432 |