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dc.contributor.author Sánchez Azqueta, Ana
dc.contributor.author Catalano Dupuy, Daniela Luján
dc.contributor.author Lopez Rivero, Arleth Susana
dc.contributor.author Tondo, Maria Laura
dc.contributor.author Orellano, Elena Graciela
dc.contributor.author Ceccarelli, Eduardo Augusto
dc.contributor.author Medina, Milagros
dc.date.available 2017-12-05T13:13:25Z
dc.date.issued 2014-06
dc.identifier.citation Sánchez Azqueta, Ana; Catalano Dupuy, Daniela Luján; Lopez Rivero, Arleth Susana; Tondo, Maria Laura; Orellano, Elena Graciela; et al.; Dynamics of the active site architecture in plant-type ferredoxin-NADP+ reductases catalytic complexes; Elsevier Science; Biochimica Et Biophysica Acta-bioenergetics; 1837; 10; 6-2014; 1730-1738
dc.identifier.issn 0005-2728
dc.identifier.uri http://hdl.handle.net/11336/29679
dc.description.abstract Kinetic isotope effects in reactions involving hydride transfer and their temperature dependence are powerful tools to explore dynamics of enzyme catalytic sites. In plant-type ferredoxin-NADP+ reductases the FAD cofactor exchanges a hydride with the NADP(H) coenzyme. Rates for these processes are considerably faster for the plastidic members (FNR) of the family than for those belonging to the bacterial class (FPR). Hydride transfer (HT) and deuteride transfer (DT) rates for the NADP+ coenzyme reduction of four plant-type FNRs (two representatives of the plastidic type FNRs and the other two from the bacterial class), and their temperature dependences are here examined applying a full tunnelling model with coupled environmental fluctuations. Parameters for the two plastidic FNRs confirm a tunnelling reaction with active dynamics contributions, but isotope effects on Arrhenius factors indicate a larger contribution for donor–acceptor distance (DAD) dynamics in the Pisum sativum FNR reaction than in the Anabaena FNR reaction. On the other hand, parameters for bacterial FPRs are consistent with passive environmental reorganisation movements dominating the HT coordinate and no contribution of DAD sampling or gating fluctuations. This indicates that active sites of FPRs are more organised and rigid than those of FNRs. These differences must be due to adaptation of the active sites and catalytic mechanisms to fulfil their particular metabolic roles, establishing a compromise between protein flexibility and functional optimisation. Analysis of site-directed mutants in plastidic enzymes additionally indicates the requirement of a minimal optimal architecture in the catalytic complex to provide a favourable gating contribution
dc.format application/pdf
dc.language.iso eng
dc.publisher Elsevier Science
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject FERREDOXIN-NADP+ REDUCTASE
dc.subject FLAVOENZYME
dc.subject KINETIC ISOTOPE EFFECT
dc.subject HYDRIDE TRANSFER
dc.subject CHARGE-TRANSFER COMPLEX
dc.subject PLASTIDIC-TYPE FNR
dc.subject BACTERIAL-TYPE FPR
dc.subject.classification Otras Ciencias Biológicas
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title Dynamics of the active site architecture in plant-type ferredoxin-NADP+ reductases catalytic complexes
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2017-12-04T19:16:45Z
dc.journal.volume 1837
dc.journal.number 10
dc.journal.pagination 1730-1738
dc.journal.pais Países Bajos
dc.journal.ciudad Amsterdam
dc.description.fil Fil: Sánchez Azqueta, Ana. Universidad de Zaragoza; España
dc.description.fil Fil: Catalano Dupuy, Daniela Luján. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil Fil: Lopez Rivero, Arleth Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil Fil: Tondo, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil Fil: Orellano, Elena Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil Fil: Ceccarelli, Eduardo Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
dc.description.fil Fil: Medina, Milagros. Universidad de Zaragoza; España
dc.journal.title Biochimica Et Biophysica Acta-bioenergetics
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005272814005118
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbabio.2014.06.003


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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)