Oxygenases: mechanisms and structural motifs for O(2) activation.
T. Bugg. Curr Opin Chem Biol, 5 (5):
550--555(October 2001)
Abstract
Recent structural and mechanistic analysis of oxygenase enzymes together
with the study of biomimetic model reactions have provided new insights
into the catalytic mechanisms of oxygenase-catalysed reactions.
High-valent iron-oxo intermediates have been implicated in heme-
and pterin-dependent mono-oxygenases. Structural motifs have been
identified for binding of non-heme iron(II) (His,His,Glu) and iron(III)
(His(2)Tyr(2)) in non-heme-dependent dioxygenases, but additional
factors influencing the choice of reaction pathway are emerging
from model studies.
%0 Journal Article
%1 citeulike:519769
%A Bugg, T. D.
%C Department of Chemistry, University of Warwick, Coventry CV4 7AL,
UK. mssgv@warwick.ac.uk
%D 2001
%J Curr Opin Chem Biol
%K mechanism oxygenases
%N 5
%P 550--555
%T Oxygenases: mechanisms and structural motifs for O(2) activation.
%U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11578928
%V 5
%X Recent structural and mechanistic analysis of oxygenase enzymes together
with the study of biomimetic model reactions have provided new insights
into the catalytic mechanisms of oxygenase-catalysed reactions.
High-valent iron-oxo intermediates have been implicated in heme-
and pterin-dependent mono-oxygenases. Structural motifs have been
identified for binding of non-heme iron(II) (His,His,Glu) and iron(III)
(His(2)Tyr(2)) in non-heme-dependent dioxygenases, but additional
factors influencing the choice of reaction pathway are emerging
from model studies.
@article{citeulike:519769,
abstract = {Recent structural and mechanistic analysis of oxygenase enzymes together
with the study of biomimetic model reactions have provided new insights
into the catalytic mechanisms of oxygenase-catalysed reactions.
High-valent iron-oxo intermediates have been implicated in heme-
and pterin-dependent mono-oxygenases. Structural motifs have been
identified for binding of non-heme iron(II) (His,His,Glu) and iron(III)
(His(2)Tyr(2)) in non-heme-dependent dioxygenases, but additional
factors influencing the choice of reaction pathway are emerging
from model studies.},
added-at = {2007-02-02T11:54:15.000+0100},
address = {Department of Chemistry, University of Warwick, Coventry CV4 7AL,
UK. mssgv@warwick.ac.uk},
author = {Bugg, T. D.},
biburl = {https://www.bibsonomy.org/bibtex/2bc04df352435ec9e4c9590825457a4f8/robert},
citeulike-article-id = {519769},
interhash = {61ce282746a40dfbaff5fcb483c4fed0},
intrahash = {bc04df352435ec9e4c9590825457a4f8},
issn = {1367-5931},
journal = {Curr Opin Chem Biol},
keywords = {mechanism oxygenases},
month = {October},
number = 5,
pages = {550--555},
priority = {2},
timestamp = {2007-02-02T11:54:15.000+0100},
title = {Oxygenases: mechanisms and structural motifs for O(2) activation.},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=11578928},
volume = 5,
year = 2001
}