Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase.

@article{Mayfield2010ComprehensiveSS,
  title={Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase.},
  author={Jeffery A. Mayfield and Rosanne E. Frederick and Bennett R. Streit and Timothy A Wencewicz and David P. Ballou and Jennifer L DuBois},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 40},
  pages={30375-88}
}
Many siderophores used for the uptake and intracellular storage of essential iron contain hydroxamate chelating groups. Their biosyntheses are typically initiated by hydroxylation of the primary amine side chains of l-ornithine or l-lysine. This reaction is catalyzed by members of a widespread family of FAD-dependent monooxygenases. Here the kinetic mechanism for a representative family member has been extensively characterized by steady state and transient kinetic methods, using heterologously… CONTINUE READING