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...
| Main Authors: | , |
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| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
American Chemical Society
2013
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| Online Access: | http://hdl.handle.net/1721.1/76212 https://orcid.org/0000-0002-2693-4982 |