Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase.

@article{Whittington2001XenonAH,
  title={Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase.},
  author={Douglas A. Whittington and Amy C Rosenzweig and Christin A. Frederick and Stephen J Lippard},
  journal={Biochemistry},
  year={2001},
  volume={40 12},
  pages={3476-82}
}
To investigate the role of protein cavities in facilitating movement of the substrates, methane and dioxygen, in the soluble methane monooxygenase hydroxylase (MMOH), we determined the X-ray structures of MMOH from Methylococcus capsulatus (Bath) cocrystallized with dibromomethane or iodoethane, or by using crystals pressurized with xenon gas. The halogenated alkanes bind in two cavities within the alpha-subunit that extend from one surface of the protein to the buried dinuclear iron active… CONTINUE READING