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J. Biol. Chem., Vol. 263, Issue 22, 10553-10556, Aug, 1988
BG Fox, KK Surerus, E Munck and JD Lipscomb
Mossbauer and EPR studies of a highly active hydroxylase component of
methane monooxygenase isolated from Methylosinus trichosporium OB3b are
reported. The Mossbauer spectra of the oxidized (as isolated) hydroxylase
show iron in a diamagnetic cluster containing an even number of Fe3+ sites.
The parameters are consistent with an antiferromagnetically coupled
binuclear cluster similar to those of hemerythrin and purple acid
phosphatases. Upon partial reduction of the hydroxylase, an S = 1/2 EPR
spectrum with g values at 1.94, 1.86, and 1.75 (gav = 1.85) is observed.
Such spectra are characteristic of oxo- bridged iron dimers in the mixed
valent Fe(II).Fe(III) state. Further reduction leads to the appearance of a
novel EPR resonance at g = 15. Comparison with an inorganic model compound
for mu-oxo-bridged binuclear iron suggests that the g = 15 signal is
characteristic of the doubly reduced state of the cluster in the protein.
In this state, the Mossbauer spectra exhibit two quadrupole doublets
typical of high spin Fe2+, consistent with the Fe(II).Fe(II) form of the
cluster. The spectral features of the iron center of the hydroxylase in
three oxidation states are all similar to those reported for mu-oxo (or mu-
hydroxo)-bridged binuclear iron clusters. Since no known monooxygenase
contains such a cluster, a new oxygenase mechanism is suggested. Three
different preparative methods yielded hydroxylases spanning a 9-fold range
in specific activity, yet the same cluster concentration and spectral
characteristics were observed. Thus, other parameters than those measured
here have a major influence on the activity.
Evidence for a mu-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase. Mossbauer and EPR studies
Department of Biochemistry, Medical School, University of Minnesota, Minneapolis 55455.
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