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Lah, Myoung Soo
Nanoporous Materials Lab
Research Interests
  • Metal-Organic Frameworks (MOFs)
  • Crystal Engineering
  • Supramolecular coordination chemistry

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THE MOBILE FLAVIN OF 4-OH BENZOATE HYDROXYLASE

Cited 132 times inthomson ciCited 126 times inthomson ci
Title
THE MOBILE FLAVIN OF 4-OH BENZOATE HYDROXYLASE
Author
GATTI, DLPALFEY, BALah, Myoung SooENTSCH, BMASSEY, VBALLOU, DPLUDWIG, ML
Keywords
PARA-HYDROXYBENZOATE HYDROXYLASE; CRYSTAL-STRUCTURE; PSEUDOMONAS-FLUORESCENS; CONFORMATIONAL CHANGE; ACTIVE-SITE; RESOLUTION; CHEMISTRY; MECHANISM
Issue Date
1994-10
Publisher
AMER ASSOC ADVANCEMENT SCIENCE
Citation
SCIENCE, v.266, no.5182, pp.110 - 114
Abstract
Para-hydroxybenzoate hydroxylase inserts oxygen into substrates by means of the labile intermediate, flavin C(4a)-hydroperoxide. This reaction requires transient isolation of the flavin and substrate from the bulk solvent. Previous crystal structures have revealed the position of the substrate para-hydroxybenzoate during oxygenation but not how it enters the active site. In this study, enzyme structures with the flavin ring displaced relative to the protein were determined, and it was established that these or similar flavin conformations also occur in solution. Movement of the flavin appears to be essential for the translocation of substrates and products into the solvent-shielded active site during catalysis.
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DOI
10.1126/science.7939628
ISSN
0036-8075
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PHY_Journal Papers
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