Photosynthetic Protein Complexes 2008
DOI: 10.1002/9783527623464.ch8
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Plastocyanin and Cytochromec6: the Soluble Electron Carriers between the Cytochromeb6fComplex and Photosystem I

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Cited by 14 publications
(14 citation statements)
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“…In addition, the reduction of diatom PSI by the strongly acidic Cyt from green alga showed an increased affinity and k ET but a lower efficiency in the formation of the properly arranged Cyt/PSI complex as compared with the native Cyt, because the too strong electrostatic interactions [17]. Thus, Chlamydomonas Pc mutants are here designed by replacing negative groups of the acidic patch -widely accepted to be responsible for electrostatic interactions with PSI [12,35,47] -by neutral or positive residues (Fig. 3).…”
Section: Discussionmentioning
confidence: 97%
See 1 more Smart Citation
“…In addition, the reduction of diatom PSI by the strongly acidic Cyt from green alga showed an increased affinity and k ET but a lower efficiency in the formation of the properly arranged Cyt/PSI complex as compared with the native Cyt, because the too strong electrostatic interactions [17]. Thus, Chlamydomonas Pc mutants are here designed by replacing negative groups of the acidic patch -widely accepted to be responsible for electrostatic interactions with PSI [12,35,47] -by neutral or positive residues (Fig. 3).…”
Section: Discussionmentioning
confidence: 97%
“…This behavior could be explained by the different intrinsic efficiency of cofactors -exposed heme vs. a hindered Cu cofactor -or different surface steric properties. From the solved crystal structure of Phaeodactylum Cyt, turns out that this protein has evolved towards a decrease in the acidic area thought to be involved in the interaction with PSI (revised in [47], and see [8,17]) (Fig. 3).…”
Section: Kinetic Analysismentioning
confidence: 97%
“…Buen ejemplo de ello es la sustitución gradual, forzada por las disponibilidades relativas de hierro y cobre, del citocromo c6 por la plastocianina en la cadena de transporte fotosintética. Las dos proteínas poseen estructuras totalmente diferentes -el citocromo es una proteína hemínica, con cuatro hélices alfa, en tanto que la plastocianina es una proteina de cobre, en forma de barril beta (ver figura)-pero juegan el mismo papel fisiológico: la transferencia de electrones, en el interior del tilacoide, entre dos complejos de membrana, el citocromo b6f y el fotosistema I (3)(4)(5). Hace unos 3.500 millones años, las cianobacterias, que fueron los primeros organismos fotosintéticos en liberar oxígeno molecular, utilizaban citocromo c6 como transportador de electrones, ya que el hierro estaba fácilmente accesible.…”
Section: Discussionunclassified
“…Al final de la evolución, las plantas superiores sólo producen plastocianina (4). La sustitución funcional de una proteína por otra es posible, a pesar de su diferencia estructural, porque ambas poseen el mismo potencial redox y punto isoeléctrico, así como áreas superficiales electrostáticas e hidrófobas equivalentes que les permiten reconocer e interaccionar con los mismos complejos de membrana (5,6). Se trata, por tanto, de un caso paradigmático de evolución convergente, a nivel molecular, gobernado por las condiciones geoquímicas cambiantes, es decir, por las biodisponibilidades relativas de ciertos elementos metálicos (3,5).…”
Section: Discussionunclassified
“…Although a lipophilic electron carrier, quinone, functions as a mediator between PS II and the cyt bf complex, the electron transfer (ET) reaction from the latter complex to PS I is conducted by soluble metal-containing carriers of cyt c 6 and/or plastocyanin (Hervás et al 1995;Hope 2000;Dîaz-Quintana et al 2008). These carriers diffuse over a relatively long distance searching for their reaction partners within the lumen side of thylakoids (see Fig.…”
Section: Introductionmentioning
confidence: 99%