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.
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