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

@article{citeulike:2997257, 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 alpha-subunit that extend from one surface of the protein to the buried dinuclear iron active site. Two additional binding sites were located in the beta-subunit. Pressurization of two crystal forms of MMOH with xenon resulted in the identification of six binding sites located exclusively in the alpha-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.}, address = {Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.}, author = {Whittington, D. A. and Rosenzweig, A. C. and Frederick, C. A. and Lippard, S. J. }, citeulike-article-id = {2997257}, issn = {0006-2960}, journal = {Biochemistry}, keywords = {xenon}, month = {March}, number = {12}, pages = {3476--3482}, posted-at = {2008-07-13 13:59:15}, priority = {2}, title = {Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11297413}, volume = {40}, year = {2001} }

TY - JOUR ID - citeulike:2997257 L3 - citeulike-article-id:2997257 TI - Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase. JF - Biochemistry VL - 40 IS - 12 SP - 3476 EP - 3482 AD - Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA. SN - 0006-2960 N2 - 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 site. Two additional binding sites were located in the beta-subunit. Pressurization of two crystal forms of MMOH with xenon resulted in the identification of six binding sites located exclusively in the alpha-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. KW - xenon AU - Whittington, DA AU - Rosenzweig, AC AU - Frederick, CA AU - Lippard, SJ PY - 2001/03/27/ UR - http://view.ncbi.nlm.nih.gov/pubmed/11297413 ER -