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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/1659

Título: Synechocystis ferredoxin/ferredoxin-NADP+-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking
Autor: Moura, José J. G.
Palma, P. Nuno
Lagoutte, Bernard
Krippahl, Ludwig
Guerlesquin, Françoise
Palavras-chave: Ferredoxin
Ferredoxin NADP+-reductase
Docking and NMR
Issue Date: 2005
Editora: Elsevier B.V. on behalf of the Federation of European Biochemical Societies
Resumo: Abstract Ferredoxin (Fd) and ferredoxin-NADP+-reductase(FNR) are two terminal physiological partners of the photosynthetic electron transport chain. Based on a nuclear magnetic resonance(NMR)-restrained-docking approach, two alternative structural models of the Fd–FNR complex in the presence of NADP+ are proposed. The protein docking simulations were performed with the software BiGGER. NMR titration revealed a 1:1 stoichiometry for the complex and allowed the mapping of the interacting residues at the surface of Fd. The NMR chemical shifts were encoded into distance constraints and used with theoretically calculated electronic coupling between the redox cofactors to propose experimentally validated docked complexes.
Descrição: FEBS Letters 579 (2005) 4585–4590
URI: http://hdl.handle.net/10362/1659
Appears in Collections:FCT: DQ - Artigos em revista internacional com arbitragem científica

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