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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. The present study examines these cavities as a potent...

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Autors principals: McCormick, Michael S., Lippard, Stephen J.
Format: Artigo
Idioma:Inglês
Publicat: 2011
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC3243792/
https://ncbi.nlm.nih.gov/pubmed/22136180
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi201248b
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