An evolutionary analysis of the reaction mechanisms of photosystem I reduction by cytochrome c6 and plastocyanin

✍ Scribed by Miguel A De la Rosa; José A Navarro; Antonio Dı́az-Quintana; Berta De la Cerda; Fernando P Molina-Heredia; Alexis Balme; Piedad del S Murdoch; Irene Dı́az-Moreno; Raúl V Durán; Manuel Hervás

• Book ID: 104443884
• Publisher: Elsevier Science
• Year: 2002
• Tongue: English
• Weight: 223 KB
• Volume: 55
• Category: Article
• ISSN: 1567-5394
• DOI: 10.1016/s1567-5394(01)00136-0

✦ Synopsis

Photosystem I reduction by the soluble metalloproteins cytochrome c 6 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 c 6 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.