Biomedical Engineering Reference
In-Depth Information
First
two
complexes
with
a
(III)
core
(I) and
(II), were isolated and
characterized
,2-peroxo)bis(-
carboxylato)diiron(III)model for the peroxo intermediate in the methane monooxygenase
hydroxylase reaction cycle is presented in Fig, 6.3.
The M
(Zang
et
al.,
1995).
Structure
of
a
(-
1
ssbauer spectrum and magnetic susceptibility proved diiron structure of the
complex and found it to be similar to that in methane monooxygenase and relative
enzymes. The crystal structures of synthetic diiron complexes of modeling compounds P
and Q in the active site of MMO have been reported. Kim and Lippard (1996) have
synthesized and structurally characterized a model for the peroxo intermediate in the
methane monooxygenase hydroxylase reaction cycle, the complex
where pz' = 3.5-bis(isopropyl)-pyrazol. In the complex, the
two iron atoms are linked by two bridging phenyl acetate ligands and a peroxoligand is
coordinated in a
ö
fashion. The transient complex [Fe2(O)2(5-MeTPA)2]
(ClO4)3,
TPA = tris2-(pyridylmethyl)amin, has been detected in reaction of H2O2 with
a
(Dong et al., 1995). The structure
of the complex has been determined with the use of a set of physical methods including
ESR, magnetization, EXAFS, X-absorption, Mössbauer and Raman spectroscopy. These
properties consisted of a valence-delocalized low-spin
pair coupled by both Heisenberg and double exchanges.
(III)TPA complex in
at
-40 °C
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