BROWSE

Related Researcher

Author's Photo

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

ITEM VIEW & DOWNLOAD

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
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.
URI
https://scholarworks.unist.ac.kr/handle/201301/6109
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0027999378
DOI
10.1126/science.7939628
ISSN
0036-8075
Appears in Collections:
CHM_Journal Papers
Files in This Item:
There are no files associated with this item.

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qrcode

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU