EC Number   |
|---|
   1.18.1.2 | - |
| 1.18.1.2 | a multiscale modelling approach for analysis of the electron transfer process in complexes of the enzyme with both ferredoxin and flavodoxin, reactions of EC 1.19.1.1 and EC1.18.1.2, respectively. The electron transfer in FNR/ferredoxin proceedes through a bridge-mediated mechanism in a dominant protein-protein complex, where transfer of the electron is facilitated by ferredoxin loop-residues 40-49. In FNR/flavodoxin, a direct transfer between redox cofactors is observed and less complex specificity than in ferredoxin |
| 1.18.1.2 | analysis of the enzyme in complex with a synthetic peptide representing the first FNR-binding repeat from Pisum sativum Tic62, including the strictly conserved core motif KTEQPLSPYTAYDDLKPPSSPSPTKPS, based on the crystal structure PDB ID 1QG0, X-ray diffraction structure analysis at 1.7 A resolution, molecular replacement |
| 1.18.1.2 | crystal structure determination and analysis at 2.5 A resolution |
| 1.18.1.2 | crystal structure determination and analysis of leaf enzyme, free or complexed with ferredoxin, and root enzyme at 2.2-2.6 and 1.7 A resolution, respectively |
| 1.18.1.2 | crystallizations of oxidized enzyme, dithionite-reduced enzyme, 2',5'-ADP-complexed enzyme, enzyme mutants S96V, E312A, E312L, and E312Q, crystal structure determinations and analysis at 1.7-2.0 A resolution, overview |
| 1.18.1.2 | crystallizations of wild-type enzyme, ferredoxin-complexed enzyme, and enzyme mutants Y308S, complexed with NADP+ or NADPH, and Y308W, complexed with NADP+, crystal structure determinations and analysis at 1.7-2.5 A resolution, overview |
| 1.18.1.2 | crystallizations of wild-type enzyme, oxidized, or substrate-complexed, and of diverse enzyme mutants, crystal structure determination and analysis at 1.6-2.5 A resolution, overview |
| 1.18.1.2 | diffraction to 2.4 A, space group P21 |
| 1.18.1.2 | enzyme complexed with NADP+, X-ray diffraction structure determination and analysis at 2.1 A resolution |
