The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum

The photosynthetic cytochrome c550 from the marine diatom Phaeodactylum tricornutum has been purified and characterized. Cytochrome c550 is mostly obtained from the soluble cell extract in relatively large amounts. In addition, the protein appeared to be truncated in the last hydrophobic residues of...

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Autores: Bernal Bayard, Pilar, Puerto Galán, Leonor, Yruela Guerrero, Inmaculada, García Rubio, Inés, Castell, M. Carmen, Ortega Rodríguez, José María, Hervás Morón, Manuel, Navarro Carruesco, José Antonio
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2016
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/68334
Acceso en línea:http://hdl.handle.net/11441/68334
https://doi.org/10.1007/s11120-016-0327-x
Access Level:acceso abierto
Palabra clave:Cytochrome c550
Phaeodactylum
Photosystem II
EPR Hemeprotein
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repository_id_str
spelling The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutumBernal Bayard, PilarPuerto Galán, LeonorYruela Guerrero, InmaculadaGarcía Rubio, InésCastell, M. CarmenOrtega Rodríguez, José MaríaHervás Morón, ManuelNavarro Carruesco, José AntonioCytochrome c550PhaeodactylumPhotosystem IIEPR HemeproteinThe photosynthetic cytochrome c550 from the marine diatom Phaeodactylum tricornutum has been purified and characterized. Cytochrome c550 is mostly obtained from the soluble cell extract in relatively large amounts. In addition, the protein appeared to be truncated in the last hydrophobic residues of the C-terminus, both in the soluble cytochrome c550 and in the protein extracted from the membrane fraction, as deduced by mass spectrometry analysis and the comparison with the gene sequence. Interestingly, it has been described that the C-terminus of cytochrome c550 forms a hydrophobic finger involved in the interaction with photosystem II in cyanobacteria. Cytochrome c550 was almost absent in solubilized photosystem II complex samples, in contrast with the PsbO and Psb31 extrinsic subunits, thus suggesting a lower affinity of cytochrome c550 for the photosystem II complex. Under iron-limiting conditions the amount of cytochrome c550 decreases up to about 45% as compared to iron-replete cells, pointing to an iron-regulated synthesis. Oxidized cytochrome c550 has been characterized using continuous wave EPR and pulse techniques, including HYSCORE, and the obtained results have been interpreted in terms of the electrostatic charge distribution in the surroundings of the heme centre.España, MINECO BIO2012-35271, BIO2015-64169-P, MAT2011-23861 and CTQ2015-64486-RSpringer VerlagBioquímica Vegetal y Biología MolecularMinisterio de Economía y Competitividad (MINECO). España2016info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/11441/68334https://doi.org/10.1007/s11120-016-0327-xreponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésPhotosynthesis Research, 133 (1-3), 273-287.BIO2012-35271BIO2015-64169-PMAT2011-23861CTQ2015-64486-Rhttps://link.springer.com/content/pdf/10.1007%2Fs11120-016-0327-x.pdfinfo:eu-repo/semantics/openAccessoai:idus.us.es:11441/683342026-06-17T12:51:07Z
dc.title.none.fl_str_mv The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
title The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
spellingShingle The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
Bernal Bayard, Pilar
Cytochrome c550
Phaeodactylum
Photosystem II
EPR Hemeprotein
title_short The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
title_full The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
title_fullStr The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
title_full_unstemmed The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
title_sort The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
dc.creator.none.fl_str_mv Bernal Bayard, Pilar
Puerto Galán, Leonor
Yruela Guerrero, Inmaculada
García Rubio, Inés
Castell, M. Carmen
Ortega Rodríguez, José María
Hervás Morón, Manuel
Navarro Carruesco, José Antonio
author Bernal Bayard, Pilar
author_facet Bernal Bayard, Pilar
Puerto Galán, Leonor
Yruela Guerrero, Inmaculada
García Rubio, Inés
Castell, M. Carmen
Ortega Rodríguez, José María
Hervás Morón, Manuel
Navarro Carruesco, José Antonio
author_role author
author2 Puerto Galán, Leonor
Yruela Guerrero, Inmaculada
García Rubio, Inés
Castell, M. Carmen
Ortega Rodríguez, José María
Hervás Morón, Manuel
Navarro Carruesco, José Antonio
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Ministerio de Economía y Competitividad (MINECO). España
dc.subject.none.fl_str_mv Cytochrome c550
Phaeodactylum
Photosystem II
EPR Hemeprotein
topic Cytochrome c550
Phaeodactylum
Photosystem II
EPR Hemeprotein
description The photosynthetic cytochrome c550 from the marine diatom Phaeodactylum tricornutum has been purified and characterized. Cytochrome c550 is mostly obtained from the soluble cell extract in relatively large amounts. In addition, the protein appeared to be truncated in the last hydrophobic residues of the C-terminus, both in the soluble cytochrome c550 and in the protein extracted from the membrane fraction, as deduced by mass spectrometry analysis and the comparison with the gene sequence. Interestingly, it has been described that the C-terminus of cytochrome c550 forms a hydrophobic finger involved in the interaction with photosystem II in cyanobacteria. Cytochrome c550 was almost absent in solubilized photosystem II complex samples, in contrast with the PsbO and Psb31 extrinsic subunits, thus suggesting a lower affinity of cytochrome c550 for the photosystem II complex. Under iron-limiting conditions the amount of cytochrome c550 decreases up to about 45% as compared to iron-replete cells, pointing to an iron-regulated synthesis. Oxidized cytochrome c550 has been characterized using continuous wave EPR and pulse techniques, including HYSCORE, and the obtained results have been interpreted in terms of the electrostatic charge distribution in the surroundings of the heme centre.
publishDate 2016
dc.date.none.fl_str_mv 2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11441/68334
https://doi.org/10.1007/s11120-016-0327-x
url http://hdl.handle.net/11441/68334
https://doi.org/10.1007/s11120-016-0327-x
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Photosynthesis Research, 133 (1-3), 273-287.
BIO2012-35271
BIO2015-64169-P
MAT2011-23861
CTQ2015-64486-R
https://link.springer.com/content/pdf/10.1007%2Fs11120-016-0327-x.pdf
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer Verlag
publisher.none.fl_str_mv Springer Verlag
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.300719

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