Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin

Autores
Nicoletti, Francesco P.; Bustamante, Juan Pablo; Droghetti, Enrica; Howes, Barry D.; Fittipaldi, Maria; Bonamore, Alessandra; Baiocco, Paola; Feis, Alessandro; Boffi, Alberto; Estrin, Dario Ariel; Smulevich, Giulietta
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The unique architecture of the active site of Thermobifida fusca truncated hemoglobin (Tf-trHb) and other globins belonging to the same family has stimulated extensive studies aimed at understanding the interplay between iron-bound ligands and distal amino acids. The behavior of the heme-bound hydroxyl, in particular, has generated much interest in view of the relationships between the spin-state equilibrium of the ferric iron atom and hydrogen-bonding capabilities (as either acceptor or donor) of the OH− group itself. The present investigation offers a detailed molecular dynamics and spectroscopic picture of the hydroxyl complexes of the WT protein and a combinatorial set of mutants, in which the distal polar residues, TrpG8, TyrCD1, and TyrB10, have been singly, doubly, or triply replaced by a Phe residue. Each mutant is characterized by a complex interplay of interactions in which the hydroxyl ligand may act both as a H-bond donor or acceptor. The resonance Raman stretching frequencies of the Fe−OH moiety, together with electron paramagnetic resonance spectra and MD simulations on each mutant, have enabled the identification of specific contributions to the unique ligand-inclusive H-bond network typical of this globin family.
Fil: Nicoletti, Francesco P.. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Droghetti, Enrica. Universita Degli Studi Di Firenze; Italia
Fil: Howes, Barry D.. Universita Degli Studi Di Firenze; Italia
Fil: Fittipaldi, Maria. Universita Degli Studi Di Firenze; Italia
Fil: Bonamore, Alessandra. Universita Di Roma; Italia
Fil: Baiocco, Paola. Italian Institute of Technology; Italia
Fil: Feis, Alessandro. Universita Degli Studi Di Firenze; Italia
Fil: Boffi, Alberto. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Smulevich, Giulietta. Universita Degli Studi Di Firenze; Italia
Materia
Hydroxyl Ligand Stabilization
Truncated Hemoglobin
Resonance Raman
Molecular Dynamic Simulations
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/31903
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/31903
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated HemoglobinNicoletti, Francesco P.Bustamante, Juan PabloDroghetti, EnricaHowes, Barry D.Fittipaldi, MariaBonamore, AlessandraBaiocco, PaolaFeis, AlessandroBoffi, AlbertoEstrin, Dario ArielSmulevich, GiuliettaHydroxyl Ligand StabilizationTruncated HemoglobinResonance RamanMolecular Dynamic Simulationshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The unique architecture of the active site of Thermobifida fusca truncated hemoglobin (Tf-trHb) and other globins belonging to the same family has stimulated extensive studies aimed at understanding the interplay between iron-bound ligands and distal amino acids. The behavior of the heme-bound hydroxyl, in particular, has generated much interest in view of the relationships between the spin-state equilibrium of the ferric iron atom and hydrogen-bonding capabilities (as either acceptor or donor) of the OH− group itself. The present investigation offers a detailed molecular dynamics and spectroscopic picture of the hydroxyl complexes of the WT protein and a combinatorial set of mutants, in which the distal polar residues, TrpG8, TyrCD1, and TyrB10, have been singly, doubly, or triply replaced by a Phe residue. Each mutant is characterized by a complex interplay of interactions in which the hydroxyl ligand may act both as a H-bond donor or acceptor. The resonance Raman stretching frequencies of the Fe−OH moiety, together with electron paramagnetic resonance spectra and MD simulations on each mutant, have enabled the identification of specific contributions to the unique ligand-inclusive H-bond network typical of this globin family.Fil: Nicoletti, Francesco P.. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Droghetti, Enrica. Universita Degli Studi Di Firenze; ItaliaFil: Howes, Barry D.. Universita Degli Studi Di Firenze; ItaliaFil: Fittipaldi, Maria. Universita Degli Studi Di Firenze; ItaliaFil: Bonamore, Alessandra. Universita Di Roma; ItaliaFil: Baiocco, Paola. Italian Institute of Technology; ItaliaFil: Feis, Alessandro. Universita Degli Studi Di Firenze; ItaliaFil: Boffi, Alberto. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; ArgentinaFil: Smulevich, Giulietta. Universita Degli Studi Di Firenze; ItaliaAmerican Chemical Society2014-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/31903Smulevich, Giulietta; Estrin, Dario Ariel; Boffi, Alberto; Feis, Alessandro; Baiocco, Paola; Bonamore, Alessandra; et al.; Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin; American Chemical Society; Biochemistry; 53; 51; 12-2014; 8021-80300006-2960CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1021/bi501132ainfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/bi501132ainfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-10T13:09:11Zoai:ri.conicet.gov.ar:11336/31903instacron: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:34982025-09-10 13:09:11.945CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin
title Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin
spellingShingle Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin
Nicoletti, Francesco P.
Hydroxyl Ligand Stabilization
Truncated Hemoglobin
Resonance Raman
Molecular Dynamic Simulations
title_short Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin
title_full Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin
title_fullStr Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin
title_full_unstemmed Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin
title_sort Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin
dc.creator.none.fl_str_mv Nicoletti, Francesco P.
Bustamante, Juan Pablo
Droghetti, Enrica
Howes, Barry D.
Fittipaldi, Maria
Bonamore, Alessandra
Baiocco, Paola
Feis, Alessandro
Boffi, Alberto
Estrin, Dario Ariel
Smulevich, Giulietta
author Nicoletti, Francesco P.
author_facet Nicoletti, Francesco P.
Bustamante, Juan Pablo
Droghetti, Enrica
Howes, Barry D.
Fittipaldi, Maria
Bonamore, Alessandra
Baiocco, Paola
Feis, Alessandro
Boffi, Alberto
Estrin, Dario Ariel
Smulevich, Giulietta
author_role author
author2 Bustamante, Juan Pablo
Droghetti, Enrica
Howes, Barry D.
Fittipaldi, Maria
Bonamore, Alessandra
Baiocco, Paola
Feis, Alessandro
Boffi, Alberto
Estrin, Dario Ariel
Smulevich, Giulietta
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Hydroxyl Ligand Stabilization
Truncated Hemoglobin
Resonance Raman
Molecular Dynamic Simulations
topic Hydroxyl Ligand Stabilization
Truncated Hemoglobin
Resonance Raman
Molecular Dynamic Simulations
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 unique architecture of the active site of Thermobifida fusca truncated hemoglobin (Tf-trHb) and other globins belonging to the same family has stimulated extensive studies aimed at understanding the interplay between iron-bound ligands and distal amino acids. The behavior of the heme-bound hydroxyl, in particular, has generated much interest in view of the relationships between the spin-state equilibrium of the ferric iron atom and hydrogen-bonding capabilities (as either acceptor or donor) of the OH− group itself. The present investigation offers a detailed molecular dynamics and spectroscopic picture of the hydroxyl complexes of the WT protein and a combinatorial set of mutants, in which the distal polar residues, TrpG8, TyrCD1, and TyrB10, have been singly, doubly, or triply replaced by a Phe residue. Each mutant is characterized by a complex interplay of interactions in which the hydroxyl ligand may act both as a H-bond donor or acceptor. The resonance Raman stretching frequencies of the Fe−OH moiety, together with electron paramagnetic resonance spectra and MD simulations on each mutant, have enabled the identification of specific contributions to the unique ligand-inclusive H-bond network typical of this globin family.
Fil: Nicoletti, Francesco P.. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Droghetti, Enrica. Universita Degli Studi Di Firenze; Italia
Fil: Howes, Barry D.. Universita Degli Studi Di Firenze; Italia
Fil: Fittipaldi, Maria. Universita Degli Studi Di Firenze; Italia
Fil: Bonamore, Alessandra. Universita Di Roma; Italia
Fil: Baiocco, Paola. Italian Institute of Technology; Italia
Fil: Feis, Alessandro. Universita Degli Studi Di Firenze; Italia
Fil: Boffi, Alberto. 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. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química, Física de los Materiales, Medioambiente y Energía; Argentina
Fil: Smulevich, Giulietta. Universita Degli Studi Di Firenze; Italia
description The unique architecture of the active site of Thermobifida fusca truncated hemoglobin (Tf-trHb) and other globins belonging to the same family has stimulated extensive studies aimed at understanding the interplay between iron-bound ligands and distal amino acids. The behavior of the heme-bound hydroxyl, in particular, has generated much interest in view of the relationships between the spin-state equilibrium of the ferric iron atom and hydrogen-bonding capabilities (as either acceptor or donor) of the OH− group itself. The present investigation offers a detailed molecular dynamics and spectroscopic picture of the hydroxyl complexes of the WT protein and a combinatorial set of mutants, in which the distal polar residues, TrpG8, TyrCD1, and TyrB10, have been singly, doubly, or triply replaced by a Phe residue. Each mutant is characterized by a complex interplay of interactions in which the hydroxyl ligand may act both as a H-bond donor or acceptor. The resonance Raman stretching frequencies of the Fe−OH moiety, together with electron paramagnetic resonance spectra and MD simulations on each mutant, have enabled the identification of specific contributions to the unique ligand-inclusive H-bond network typical of this globin family.
publishDate 2014
dc.date.none.fl_str_mv 2014-12
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/11336/31903
Smulevich, Giulietta; Estrin, Dario Ariel; Boffi, Alberto; Feis, Alessandro; Baiocco, Paola; Bonamore, Alessandra; et al.; Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin; American Chemical Society; Biochemistry; 53; 51; 12-2014; 8021-8030
0006-2960
CONICET Digital
CONICET
url http://hdl.handle.net/11336/31903
identifier_str_mv Smulevich, Giulietta; Estrin, Dario Ariel; Boffi, Alberto; Feis, Alessandro; Baiocco, Paola; Bonamore, Alessandra; et al.; Interplay of the H-Bond Donor–Acceptor Role of the Distal Residues in Hydroxyl Ligand Stabilization of Thermobifida fusca Truncated Hemoglobin; American Chemical Society; Biochemistry; 53; 51; 12-2014; 8021-8030
0006-2960
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/bi501132a
info:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/bi501132a
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 American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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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score 12.993085

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