The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes

The resonance Raman spectra of the Pr state of the N-terminal 65-kDa fragment of plant phytochrome phyA have been measured and analyzed in terms of the configuration and conformation of the tetrapyrroles methine bridges. Spectra were obtained from phyA adducts reconstituted with the natural chromoph...

Descripción completa

Detalles Bibliográficos
Autores: Murgida, Daniel Horacio, von Stetten, David, Hildebrandt, Peter, Schwinté, Pascale, Siebert, Friedrich, Sharda, Shivani, Gärtner, Wolfgang, Mroginski, Maria Andrea
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2007
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/103445
Acceso en línea:http://hdl.handle.net/11336/103445
Access Level:acceso abierto
Palabra clave:Phytochrome
Photoreceptors
FT-Raman
DFT simulations
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
id AR_43fd34f6002e916af8a8fec8eb152cd4
oai_identifier_str oai:ri.conicet.gov.ar:11336/103445
network_acronym_str AR
network_name_str Argentina
repository_id_str
dc.title.none.fl_str_mv The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes
title The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes
spellingShingle The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes
Murgida, Daniel Horacio
Phytochrome
Photoreceptors
FT-Raman
DFT simulations
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
title_short The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes
title_full The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes
title_fullStr The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes
title_full_unstemmed The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes
title_sort The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes
dc.creator.none.fl_str_mv Murgida, Daniel Horacio
von Stetten, David
Hildebrandt, Peter
Schwinté, Pascale
Siebert, Friedrich
Sharda, Shivani
Gärtner, Wolfgang
Mroginski, Maria Andrea
author Murgida, Daniel Horacio
author_facet Murgida, Daniel Horacio
von Stetten, David
Hildebrandt, Peter
Schwinté, Pascale
Siebert, Friedrich
Sharda, Shivani
Gärtner, Wolfgang
Mroginski, Maria Andrea
author_role author
author2 von Stetten, David
Hildebrandt, Peter
Schwinté, Pascale
Siebert, Friedrich
Sharda, Shivani
Gärtner, Wolfgang
Mroginski, Maria Andrea
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Phytochrome
Photoreceptors
FT-Raman
DFT simulations
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
topic Phytochrome
Photoreceptors
FT-Raman
DFT simulations
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
description The resonance Raman spectra of the Pr state of the N-terminal 65-kDa fragment of plant phytochrome phyA have been measured and analyzed in terms of the configuration and conformation of the tetrapyrroles methine bridges. Spectra were obtained from phyA adducts reconstituted with the natural chromophore phytochromobilin as well as phycocyanobilin and its isotopomers labeled at the terminal methine bridges through C-13/C-12 and D/H substitution. Upon comparing the resonance Raman spectra of the various phyA adducts, it was possible to identify the bands that originate from normal modes dominated by the stretching coordinates of the terminal methine bridges A-B and C-D. Quantum chemical calculations of the isolated tetrapyrroles reveal that these modes are sensitive indicators for the methine bridge configuration and conformation. For all phyA adducts, the experimental spectra of Pr including this marker band region are well reproduced by the calculated spectra obtained for the ZZZasa configuration. In contrast, there are substantial discrepancies between the experimental spectra and the spectra calculated for the ZZZssa configuration, which has been previously shown to be the chromophore geometry in the Pr state of the bacterial, biliverdin-binding phytochrome from Deinococcus radiodurans (Wagner, J. R., J. S. Brunzelle, K. T. Forest, R. D. Vierstra. 2005. Nature. 438: 325-331). The results of this work, therefore, suggest that plant and bacterial (biliverdin-binding) phytochromes exhibit different structures in the parent state although the mechanism of the photoinduced reaction cycle may be quite similar.
publishDate 2007
dc.date.none.fl_str_mv 2007-10
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/11336/103445
Murgida, Daniel Horacio; von Stetten, David; Hildebrandt, Peter; Schwinté, Pascale; Siebert, Friedrich; et al.; The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes; Cell Press; Biophysical Journal; 93; 7; 10-2007; 2410-2417
0006-3495
CONICET Digital
CONICET
url http://hdl.handle.net/11336/103445
identifier_str_mv Murgida, Daniel Horacio; von Stetten, David; Hildebrandt, Peter; Schwinté, Pascale; Siebert, Friedrich; et al.; The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes; Cell Press; Biophysical Journal; 93; 7; 10-2007; 2410-2417
0006-3495
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349507714960
info:eu-repo/semantics/altIdentifier/doi/10.1529/biophysj.107.108092
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 Cell Press
publisher.none.fl_str_mv Cell Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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
_version_ 1799195622799048704
spelling The Chromophore Structures of the Pr States in Plant and Bacterial PhytochromesMurgida, Daniel Horaciovon Stetten, DavidHildebrandt, PeterSchwinté, PascaleSiebert, FriedrichSharda, ShivaniGärtner, WolfgangMroginski, Maria AndreaPhytochromePhotoreceptorsFT-RamanDFT simulationshttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The resonance Raman spectra of the Pr state of the N-terminal 65-kDa fragment of plant phytochrome phyA have been measured and analyzed in terms of the configuration and conformation of the tetrapyrroles methine bridges. Spectra were obtained from phyA adducts reconstituted with the natural chromophore phytochromobilin as well as phycocyanobilin and its isotopomers labeled at the terminal methine bridges through C-13/C-12 and D/H substitution. Upon comparing the resonance Raman spectra of the various phyA adducts, it was possible to identify the bands that originate from normal modes dominated by the stretching coordinates of the terminal methine bridges A-B and C-D. Quantum chemical calculations of the isolated tetrapyrroles reveal that these modes are sensitive indicators for the methine bridge configuration and conformation. For all phyA adducts, the experimental spectra of Pr including this marker band region are well reproduced by the calculated spectra obtained for the ZZZasa configuration. In contrast, there are substantial discrepancies between the experimental spectra and the spectra calculated for the ZZZssa configuration, which has been previously shown to be the chromophore geometry in the Pr state of the bacterial, biliverdin-binding phytochrome from Deinococcus radiodurans (Wagner, J. R., J. S. Brunzelle, K. T. Forest, R. D. Vierstra. 2005. Nature. 438: 325-331). The results of this work, therefore, suggest that plant and bacterial (biliverdin-binding) phytochromes exhibit different structures in the parent state although the mechanism of the photoinduced reaction cycle may be quite similar.Fil: Murgida, Daniel Horacio. Technische Universitat Berlin; Alemania. 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: von Stetten, David. Technische Universitat Berlin; AlemaniaFil: Hildebrandt, Peter. Technische Universitat Berlin; AlemaniaFil: Schwinté, Pascale. Universidad de Friburgo; AlemaniaFil: Siebert, Friedrich. Universidad de Friburgo; AlemaniaFil: Sharda, Shivani. Max-Planck-Institut fur Bioanorganische Chemie; AlemaniaFil: Gärtner, Wolfgang. Technische Universitat Berlin; Alemania. Max-Planck-Institut fur Bioanorganische Chemie; AlemaniaFil: Mroginski, Maria Andrea. Max-Planck-Institut fur Bioanorganische Chemie; AlemaniaCell Press2007-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/103445Murgida, Daniel Horacio; von Stetten, David; Hildebrandt, Peter; Schwinté, Pascale; Siebert, Friedrich; et al.; The Chromophore Structures of the Pr States in Plant and Bacterial Phytochromes; Cell Press; Biophysical Journal; 93; 7; 10-2007; 2410-24170006-3495CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349507714960info:eu-repo/semantics/altIdentifier/doi/10.1529/biophysj.107.108092info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2024-05-08T13:58:19Zoai:ri.conicet.gov.ar:11336/103445instacron: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:34982024-05-08 13:58:19.551CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
score 15.812429

Similares en LA Referencia