<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Palma, P. N.</style></author><author><style face="normal" font="default" size="100%">Lagoutte, B.</style></author><author><style face="normal" font="default" size="100%">Krippahl, L.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Guerlesquin, F.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking</style></title><secondary-title><style face="normal" font="default" size="100%">FEBS Lett</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins/*chemistry/genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Ferredoxin-NADP Reductase/*chemistry/genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Ferredoxins/*chemistry/genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Macromolecular Substances</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">NADP/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Nuclear Magnetic Resonance, Biomolecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Alignment</style></keyword><keyword><style  face="normal" font="default" size="100%">Synechocystis/*enzymology</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Aug 29</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=16087182 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">21</style></number><volume><style face="normal" font="default" size="100%">579</style></volume><pages><style face="normal" font="default" size="100%">4585-90</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">16087182</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0014-5793 (Print)0014-5793 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">REQUIMTE, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2859-516 Caparica, Portugal.</style></auth-address></record></records></xml>