The structure at 2 angstrom resolution of Phycocyanin from Gracilaria chilensis and the energy transfer network in a PC-PC complex

Contreras-Martel, C; Matamala Á.; Bruna, C; Poo-Caamano, G; Almonacid D; Figueroa, M; Martinez-Oyanedel, J; Bunster, M

Abstract

Phycocyanin is a phycobiliprotein involved in light harvesting and conduction of light to the reaction centers in cyanobacteria and red algae. The structure of C-phycocyanin from Gracilaria chilensis was solved by X-ray crystallography at 2.0 Å resolution in space group P21. An interaction model between two PC heterohexamers was built, followed by molecular dynamic refinement. The best model showed an inter-hexamer rotation of 23°. The coordinates of a PC heterohexamer (αβ)6 and of the PC-PC complex were used to perform energy transfer calculations between chromophores pairs using the fluorescence resonance energy transfer approach (FRET). Two main intra PC (Iβ3 82 → Iα1 84 → Iα5 84 → Iβ6 82 and Iβ3 153 → Iβ5 153) and two main inter PC (Iβ6 82 → IIβ3 82 and Iβ5 153 → IIβ3 153) pathways were proposed based on the values of the energy transfer constants calculated for all the chromophore pairs in the hexamer and in the complex. © 2006 Elsevier B.V. All rights reserved.

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Título según WOS: The structure at 2 angstrom resolution of Phycocyanin from Gracilaria chilensis and the energy transfer network in a PC-PC complex
Título según SCOPUS: The structure at 2 Å resolution of Phycocyanin from Gracilaria chilensis and the energy transfer network in a PC-PC complex
Título de la Revista: BIOPHYSICAL CHEMISTRY
Volumen: 125
Número: 02-mar
Editorial: ELSEVIER SCIENCE BV
Fecha de publicación: 2007
Página de inicio: 388
Página final: 396
Idioma: English
URL: http://linkinghub.elsevier.com/retrieve/pii/S0301462206002948
DOI:

10.1016/j.bpc.2006.09.014

Notas: ISI, SCOPUS