Analysis of Substrate Access to Active Sites in Bacterial Multicomponent Monooxygenase Hydroxylases: X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase from Pseudomonas Sp Ox1
In all structurally characterized bacterial multicomponent monooxygenase (BMM) hydroxylase proteins, a series of hydrophobic cavities in the α-subunit trace a conserved path from the protein exterior to the carboxylate-bridged diiron active site. This study examines these cavities as a potential rou...
मुख्य लेखकों: | McCormick, Michael S., Lippard, Stephen J. |
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अन्य लेखक: | Massachusetts Institute of Technology. Department of Chemistry |
स्वरूप: | लेख |
भाषा: | en_US |
प्रकाशित: |
American Chemical Society
2013
|
ऑनलाइन पहुंच: | http://hdl.handle.net/1721.1/76212 https://orcid.org/0000-0002-2693-4982 |
समान संसाधन
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Multiple Roles of Component Proteins in Bacterial Multicomponent Monooxygenases: Phenol Hydroxylase and Toluene/o-Xylene Monooxygenase from Pseudomonas sp. OX1
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Structural investigations of hydroxylase proteins and complexes in bacterial multicomponent monooxygenase systems
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Characterization of a Peroxodiiron(III) Intermediate in the T201S Variant of Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas sp. OX1
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Dioxygen activation and substrate hydroxylation by the hydroxylase component of toluene/O-xylene monooxygenase from pseudomonas sporium OX1
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Insights into the different dioxygen activation pathways of methane and toluene monooxygenase hydroxylases
द्वारा: Bochevarov, Arteum D., और अन्य
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