@article {2360,
	title = {Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking},
	journal = {FEBS Lett},
	volume = {579},
	number = {21},
	year = {2005},
	note = {<p>0014-5793 (Print)0014-5793 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Aug 29},
	pages = {4585-90},
	abstract = {<p>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.</p>
},
	keywords = {*Protein Conformation, Amino Acid Sequence, Bacterial Proteins/*chemistry/genetics, Ferredoxin-NADP Reductase/*chemistry/genetics, Ferredoxins/*chemistry/genetics, Macromolecular Substances, Models, Molecular, Molecular Sequence Data, NADP/*chemistry, Nuclear Magnetic Resonance, Biomolecular, Sequence Alignment, Synechocystis/*enzymology},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=16087182 },
	author = {Palma, P. N. and Lagoutte, B. and Krippahl, L. and Moura, J. J. and Guerlesquin, F.}
}
