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Título : The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum
Autor : Bernal-Bayard, Pilar; Puerto-Galán, Leonor ; Yruela Guerrero, Inmaculada ; García-Rubio, Inés; Castell, Carmen; Ortega, José M. ; Alonso, Pablo J.; Roncel, Mercedes; Martínez, Jesús I.; Hervás, Manuel ; Navarro, José A.
Palabras clave : Cytochrome c550
Photosystem II
Fecha de publicación : 2017
Editor: Springer
Citación : Bernal-Bayard P, Puerto-Galán L, Yruela I, García-Rubio I, Castell C, Ortega JM, Alonso PJ, Roncel M, Martínez JI, Hervás M, Navarro JA. The photosynthetic cytochrome c550 from the diatom Phaeodactylum tricornutum. Photosynthesis Research 133 (1–3): 273–287 (2017)
Resumen: The photosynthetic cytochrome c550 from the marine diatom Phaeodactylum tricornutum has been purified and characterized. Cytochrome c550 is mostly obtained from the soluble cell extract in relatively large amounts. In addition, the protein appeared to be truncated in the last hydrophobic residues of the C-terminus, both in the soluble cytochrome c550 and in the protein extracted from the membrane fraction, as deduced by mass spectrometry analysis and the comparison with the gene sequence. Interestingly, it has been described that the C-terminus of cytochrome c550 forms a hydrophobic finger involved in the interaction with photosystem II in cyanobacteria. Cytochrome c550 was almost absent in solubilized photosystem II complex samples, in contrast with the PsbO and Psb31 extrinsic subunits, thus suggesting a lower affinity of cytochrome c550 for the photosystem II complex. Under iron-limiting conditions the amount of cytochrome c550 decreases up to about 45% as compared to iron-replete cells, pointing to an iron-regulated synthesis. Oxidized cytochrome c550 has been characterized using continuous wave EPR and pulse techniques, including HYSCORE, and the obtained results have been interpreted in terms of the electrostatic charge distribution in the surroundings of the heme centre.
Descripción : 44 Pags.- 1 Tabl.- 11 Figs. The definitive version is available at: https://link.springer.com/journal/11120
Versión del editor: http://dx.doi.org/10.1007/s11120-016-0327-x
URI : http://hdl.handle.net/10261/142421
DOI: 10.1007/s11120-016-0327-x
ISSN: 0166-8595
E-ISSN: 1573-5079
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