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dc.contributor.authorRosa, Miguel A. de la-
dc.contributor.authorNavarro, José A.-
dc.contributor.authorDíaz-Quintana, Antonio-
dc.contributor.authorCerda, Berta de la-
dc.contributor.authorMolina-Heredia, Fernando P.-
dc.contributor.authorBalme, Alexis-
dc.contributor.authorMurdoch, Piedad del S.-
dc.contributor.authorDíaz-Moreno, Irene-
dc.contributor.authorDurán, Raúl V.-
dc.contributor.authorHervás, Manuel-
dc.identifier.citationBioelectrochemistry 55(1-2): 41-45 (2002)en_US
dc.description8 pages, 4 figures, 1 table.-- PMID: 11786337 [PubMed].-- Available online Nov 29, 2001.en_US
dc.description.abstractPhotosystem I reduction by the soluble metalloproteins cytochrome c6 and plastocyanin, which are alternatively synthesized by some photosynthetic organisms depending on the relative availability of copper and iron, has been investigated in cyanobacteria, green algae and plants. The reaction mechanism is classified in three different types on the basis of the affinity of the membrane complex towards its electron donor protein. The role of electrostatic interactions in forming an intermediate transient complex, as well as the structural and functional similarities of cytochrome c6 and plastocyanin are analysed from an evolutionary point of view. The proposal made is that the heme protein was first “discovered” by nature, when iron was much more abundant on the Earth's surface, and replaced by plastocyanin when copper became available because of the oxidizing conditions of the new atmosphere.en_US
dc.description.sponsorshipThe research was supported by the European Union (Networks ERB-FMRX-CT98-0218 and HPRN-CT1999-00095), Spanish Ministry of Science and Technology (MCYT, Grant BMC2000-0444), and Andalusian Government (PAI, CVI-0198).en_US
dc.format.extent7450 bytes-
dc.subjectCytochrome c6en_US
dc.subjectElectron transferen_US
dc.titleAn evolutionary analysis of the reaction mechanisms of photosystem I reduction by cytochrome c(6) and plastocyaninen_US
dc.description.peerreviewedPeer revieweden_US
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