The C-terminal extension of bacterial flavodoxin-reductases: involvement in the hydride transfer mechanism from the coenzyme.

@article{Bortolotti2014TheCE,
  title={The C-terminal extension of bacterial flavodoxin-reductases: involvement in the hydride transfer mechanism from the coenzyme.},
  author={Ana Bortolotti and Ana S{\'a}nchez-Azqueta and Celia M. Maya and Adri{\'a}n Vel{\'a}zquez-Campoy and Juan A Hermoso and Milagros Medina and N{\'e}stor Cortez},
  journal={Biochimica et biophysica acta},
  year={2014},
  volume={1837 1},
  pages={33-43}
}
To study the role of the mobile C-terminal extension present in bacterial class of plant type NADP(H):ferredoxin reductases during catalysis, we generated a series of mutants of the Rhodobacter capsulatus enzyme (RcFPR). Deletion of the six C-terminal amino acids beyond alanine 266 was combined with the replacement A266Y, emulating the structure present in plastidic versions of this flavoenzyme. Analysis of absorbance and fluorescence spectra suggests that deletion does not modify the general… CONTINUE READING