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J. Biol. Chem., Vol. 276, Issue 24, 21381-21386, June 15, 2001
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From the The initial enzyme of ethylbenzene
metabolism in denitrifying Azoarcus strain EbN1,
ethylbenzene dehydrogenase, was purified and characterized. The soluble
periplasmic enzyme is the first known enzyme oxidizing a nonactivated
hydrocarbon without molecular oxygen as cosubstrate. It is a novel
molybdenum/iron-sulfur/heme protein of 155 kDa, which consists of three
subunits (96, 43, and 23 kDa) in an
Ethylbenzene Dehydrogenase, a Novel Hydrocarbon-oxidizing
Molybdenum/Iron-Sulfur/Heme Enzyme*
and Max-Planck-Institut für marine
Mikrobiologie, Celsiusstrasse 1, 28359 Bremen, and
§ Mikrobiologie, Institut für Biologie II,
Universität Freiburg, Schänzlestrasse 1,
79104 Freiburg, Germany
structure. The N-terminal
amino acid sequence of the subunit is similar to that of other
molybdenum proteins such as selenate reductase from the related species
Thauera selenatis. Ethylbenzene dehydrogenase is unique in
that it oxidizes the hydrocarbon ethylbenzene, a compound without
functional groups, to (S)-1-phenylethanol. Formation of the
product was evident by coupling to an enantiomer-specific (S)-1-phenylethanol dehydrogenase from the same organism.
The apparent Km of the enzyme for ethylbenzene is
very low at <2 µM. Oxygen does not affect ethylbenzene
dehydrogenase activity in extracts but inactivates the purified enzyme,
if the heme b cofactor is in the reduced state. A variant of
ethylbenzene dehydrogenase exhibiting significant activity also with
the homolog n-propylbenzene was detected in a related
Azoarcus strain (PbN1).
*
This work was supported by the Deutsche
Forschungsgemeinschaft and the Max-Planck-Gesellschaft.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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