New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL.

@article{Gong2000NewMI,
  title={New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL.},
  author={Weimin Gong and Bing Hao and Michael K. Chan},
  journal={Biochemistry},
  year={2000},
  volume={39 14},
  pages={3955-62}
}
The FixL heme domain serves as the dioxygen switch in the FixL/FixJ two-component system of Rhizobia. Recent structural studies of the Bradyrhizobium japonicum FixL heme domain (BjFixLH) have suggested an allosteric mechanism that is distinct from the classical hemoglobin model. To gain further insight into the FixL sensing mechanism, structures of BjFixLH bound to dioxygen, imidazole, and nitric oxide have been determined. These structures, particularly the structure of BjFixLH bound to its… CONTINUE READING