EC Number   |
|---|
  1.19.1.1 | 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 |
| 1.19.1.1 | in complex with 2'-phospho-AMP and NADP+. In the complexes obtained, the nucleotides bind exclusively through the adenosine moiety. The adenosine moiety binds into a cavity formed by residues of conserved segments, i.e residues 128 to 130, residues 158 to 163, residues 193 to 205, and residues 233 to 240. The adenosine binding site is essentially formed by residues R158, R195 and R203, which stabilise the nucleotide |
| 1.19.1.1 | molecular modelling indicates that movement of the C-terminal tryptophan (W248) is necessary to permit close approach of the nicotinamide ring of NADPH to the flavin. Residues R174 and R184 are located close to the adenosine ribose 2'-phosphate group, and R144 is likely to interact with the nicotinamide ribose 5'-phosphate group |
| 1.19.1.1 | no perturbation of the 31P-NMR resonances assigned to the FAD moiety of FNR or the FMN and phosphodiester moieties of Azotobacter flavodoxin are observed on complexation of Azotobacter flavodoxin and Spinacia oleracea FNR. Reduction of FMN to its semiquinone form results in extensive line-broadening of the FMN resonance. The FAD resonances of the FNR-flavodoxin complex are unaffected by FMN semiquinone formation. The distance from the FMN phosphate to the flavin ring is altered on binding the flavodoxin to FNR |
| 1.19.1.1 | structure to 2.5 A resolution, orthorhombic space group P21212, with unit-cell parameters a = 57.2, b = 164.3, c = 95.0 A, containing two protein molecules in the asymmetric unit |
| 1.19.1.1 | to 2.17 A resolution, tetragonal space group P41212, with unit-cell parameters a = b = 66.49, c = 121.32 A |
