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dc.contributor.author
Saigo, Mariana  
dc.contributor.author
Tronconi, Marcos Ariel  
dc.contributor.author
Gerrard Wheeler, Mariel Claudia  
dc.contributor.author
Alvarez, Clarisa Ester  
dc.contributor.author
Drincovich, Maria Fabiana  
dc.contributor.author
Andreo, Carlos Santiago  
dc.date.available
2016-10-27T21:10:55Z  
dc.date.issued
2013-07  
dc.identifier.citation
Saigo, Mariana; Tronconi, Marcos Ariel; Gerrard Wheeler, Mariel Claudia; Alvarez, Clarisa Ester; Drincovich, Maria Fabiana; et al.; Biochemical approaches to C4 photosynthesis evolution studies: the case of malic enzymes decarboxylases; Springer; Photosynthesis Research; 117; 1; 7-2013; 177-187  
dc.identifier.issn
0166-8595  
dc.identifier.uri
http://hdl.handle.net/11336/7831  
dc.description.abstract
C4 photosynthesis enables the capture of atmospheric CO2 and its concentration at the site of RuBisCO, thus counteracting the negative effects of low atmospheric levels of CO2 and high atmospheric levels of O2 (21 %) on photosynthesis. The evolution of this complex syndrome was a multistep process. It did not occur by simply recruiting pre-exiting components of the pathway from C3 ancestors which were already optimized for C4 function. Rather it involved modifications in the kinetics and regulatory properties of pre-existing isoforms of non-photosynthetic enzymes in C3 plants. Thus, biochemical studies aimed at elucidating the functional adaptations of these enzymes are central to the development of an integrative view of the C4 mechanism. In the present review, the most important biochemical approaches that we currently use to understand the evolution of the C4 isoforms of malic enzyme are summarized. It is expected that this information will help in the rational design of the best decarboxylation processes to provide CO2 for RuBisCO in engineering C3 species to perform C4 photosynthesis.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Springer  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
C4 Enzymes  
dc.subject
Malic Enzymes  
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Kinetic And Structural Properties  
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Molecular And Biochemical Technologies  
dc.subject.classification
Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Biochemical approaches to C4 photosynthesis evolution studies: the case of malic enzymes decarboxylases  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2016-03-14T12:49:07Z  
dc.journal.volume
117  
dc.journal.number
1  
dc.journal.pagination
177-187  
dc.journal.pais
Alemania  
dc.journal.ciudad
Berlin  
dc.description.fil
Fil: Saigo, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina  
dc.description.fil
Fil: Tronconi, Marcos Ariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina  
dc.description.fil
Fil: Gerrard Wheeler, Mariel Claudia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina  
dc.description.fil
Fil: Alvarez, Clarisa Ester. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina  
dc.description.fil
Fil: Drincovich, Maria Fabiana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina  
dc.description.fil
Fil: Andreo, Carlos Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Centro de Estudios Fotosintéticos y Bioquímicos (i); Argentina  
dc.journal.title
Photosynthesis Research  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://link.springer.com/article/10.1007/s11120-013-9879-1  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/ 10.1007/s11120-013-9879-1