Cytochrome c1 exhibits two binding sites for cytochrome c in plants

n plants, channeling of cytochrome c molecules between complexes III and IV has been purported to shuttle electrons within the supercomplexes instead of carrying electrons by random diffusion across the intermembrane bulk phase. However, the mode plant cytochrome c behaves inside a supercomplex such...

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Autores: Moreno Beltrán, José Blas, Díaz Quintana, Antonio Jesús, González Arzola, Katiuska, Velázquez Campoy, Adrián, Rosa Acosta, Miguel Ángel de la, Díaz Moreno, Irene
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2014
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/68192
Acceso en línea:http://hdl.handle.net/11441/68192
https://doi.org/10.1016/j.bbabio.2014.07.017
Access Level:acceso abierto
Palabra clave:Respirasome
NMR
Supercomplex
Cytochrome bc1 Complex
Arabidopsis thaliana
Cytochrome c
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spelling Cytochrome c1 exhibits two binding sites for cytochrome c in plantsMoreno Beltrán, José BlasDíaz Quintana, Antonio JesúsGonzález Arzola, KatiuskaVelázquez Campoy, AdriánRosa Acosta, Miguel Ángel de laDíaz Moreno, IreneRespirasomeNMRSupercomplexCytochrome bc1 ComplexArabidopsis thalianaCytochrome cn plants, channeling of cytochrome c molecules between complexes III and IV has been purported to shuttle electrons within the supercomplexes instead of carrying electrons by random diffusion across the intermembrane bulk phase. However, the mode plant cytochrome c behaves inside a supercomplex such as the respirasome, formed by complexes I, III and IV, remains obscure from a structural point of view. Here, we report ab-initio Brownian dynamics calculations and nuclear magnetic resonance-driven docking computations showing two binding sites for plant cytochrome c at the head soluble domain of plant cytochrome c1, namely a non-productive (or distal) site with a long heme-to-heme distance and a functional (or proximal) site with the two heme groups close enough as to allow electron transfer. As inferred from isothermal titration calorimetry experiments, the two binding sites exhibit different equilibrium dissociation constants, for both reduced and oxidized species, that are all within the micromolar range, thus revealing the transient nature of such a respiratory complex. Although the docking of cytochrome c at the distal site occurs at the interface between cytochrome c1 and the Rieske subunit, it is fully compatible with the complex III structure. In our model, the extra distal site in complex III could indeed facilitate the functional cytochrome c channeling towards complex IV by building a >floating boat bridge> of cytochrome c molecules (between complexes III and IV) in plant respirasome.Ministerio de Economía y Competitividad BFU2009-07190/BMC, BFU2010-19451/BMC, BFU2012-31670/BMCJunta de Andalucía BIO198ElsevierBioquímica Vegetal y Biología MolecularMinisterio de Economía y Competitividad (MINECO). EspañaJunta de Andalucía2014info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/11441/68192https://doi.org/10.1016/j.bbabio.2014.07.017reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésBiochimica et Biophysica Acta - Bioenergetics, 1837, 1717-1729.BFU2009-07190/BMCBFU2010-19451/BMCBFU2012-31670/BMCBIO198http://dx.doi.org/10.1016/j.bbabio.2014.07.017info:eu-repo/semantics/openAccessoai:idus.us.es:11441/681922026-06-17T12:51:07Z
dc.title.none.fl_str_mv Cytochrome c1 exhibits two binding sites for cytochrome c in plants
title Cytochrome c1 exhibits two binding sites for cytochrome c in plants
spellingShingle Cytochrome c1 exhibits two binding sites for cytochrome c in plants
Moreno Beltrán, José Blas
Respirasome
NMR
Supercomplex
Cytochrome bc1 Complex
Arabidopsis thaliana
Cytochrome c
title_short Cytochrome c1 exhibits two binding sites for cytochrome c in plants
title_full Cytochrome c1 exhibits two binding sites for cytochrome c in plants
title_fullStr Cytochrome c1 exhibits two binding sites for cytochrome c in plants
title_full_unstemmed Cytochrome c1 exhibits two binding sites for cytochrome c in plants
title_sort Cytochrome c1 exhibits two binding sites for cytochrome c in plants
dc.creator.none.fl_str_mv Moreno Beltrán, José Blas
Díaz Quintana, Antonio Jesús
González Arzola, Katiuska
Velázquez Campoy, Adrián
Rosa Acosta, Miguel Ángel de la
Díaz Moreno, Irene
author Moreno Beltrán, José Blas
author_facet Moreno Beltrán, José Blas
Díaz Quintana, Antonio Jesús
González Arzola, Katiuska
Velázquez Campoy, Adrián
Rosa Acosta, Miguel Ángel de la
Díaz Moreno, Irene
author_role author
author2 Díaz Quintana, Antonio Jesús
González Arzola, Katiuska
Velázquez Campoy, Adrián
Rosa Acosta, Miguel Ángel de la
Díaz Moreno, Irene
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Bioquímica Vegetal y Biología Molecular
Ministerio de Economía y Competitividad (MINECO). España
Junta de Andalucía
dc.subject.none.fl_str_mv Respirasome
NMR
Supercomplex
Cytochrome bc1 Complex
Arabidopsis thaliana
Cytochrome c
topic Respirasome
NMR
Supercomplex
Cytochrome bc1 Complex
Arabidopsis thaliana
Cytochrome c
description n plants, channeling of cytochrome c molecules between complexes III and IV has been purported to shuttle electrons within the supercomplexes instead of carrying electrons by random diffusion across the intermembrane bulk phase. However, the mode plant cytochrome c behaves inside a supercomplex such as the respirasome, formed by complexes I, III and IV, remains obscure from a structural point of view. Here, we report ab-initio Brownian dynamics calculations and nuclear magnetic resonance-driven docking computations showing two binding sites for plant cytochrome c at the head soluble domain of plant cytochrome c1, namely a non-productive (or distal) site with a long heme-to-heme distance and a functional (or proximal) site with the two heme groups close enough as to allow electron transfer. As inferred from isothermal titration calorimetry experiments, the two binding sites exhibit different equilibrium dissociation constants, for both reduced and oxidized species, that are all within the micromolar range, thus revealing the transient nature of such a respiratory complex. Although the docking of cytochrome c at the distal site occurs at the interface between cytochrome c1 and the Rieske subunit, it is fully compatible with the complex III structure. In our model, the extra distal site in complex III could indeed facilitate the functional cytochrome c channeling towards complex IV by building a >floating boat bridge> of cytochrome c molecules (between complexes III and IV) in plant respirasome.
publishDate 2014
dc.date.none.fl_str_mv 2014
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11441/68192
https://doi.org/10.1016/j.bbabio.2014.07.017
url http://hdl.handle.net/11441/68192
https://doi.org/10.1016/j.bbabio.2014.07.017
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Biochimica et Biophysica Acta - Bioenergetics, 1837, 1717-1729.
BFU2009-07190/BMC
BFU2010-19451/BMC
BFU2012-31670/BMC
BIO198
http://dx.doi.org/10.1016/j.bbabio.2014.07.017
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 Elsevier
publisher.none.fl_str_mv Elsevier
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 15,301603

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