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

D. A. Whittington, A. C. Rosenzweig, C. A. Frederick*, S. J. Lippard

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

Abstract

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 α-subunit that extend from one surface of the protein to the buried dinuclear iron active site. Two additional binding sites were located in the β-subunit. Pressurization of two crystal forms of MMOH with xenon resulted in the identification of six binding sites located exclusively in the α-subunit. These results indicate that hydrophobic species bind preferentially in preexisting cavities in MMOH and support the hypothesis that such cavities may play a functional role in sequestering and enhancing the availability of the physiological substrates for reaction at the active site.

Original languageEnglish (US)
Pages (from-to)3476-3482
Number of pages7
JournalBiochemistry
Volume40
Issue number12
DOIs
StatePublished - Mar 27 2001

ASJC Scopus subject areas

  • Biochemistry

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