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Originally published In Press as doi:10.1074/jbc.M304351200 on June 3, 2003
J. Biol. Chem., Vol. 278, Issue 32, 30193-30198, August 8, 2003
Novel Antioxidant Role of Alcohol Dehydrogenase E from Escherichia coli*
Pedro Echave ,
Jordi Tamarit,
Elisa Cabiscol and
Joaquim Ros
From the
Departament de Ciències Mèdiques Bàsiques, Facultat
de Medicina, Universitat de Lleida, 25198 Lleida, Spain
Alcohol dehydrogenase E (AdhE) is an Fe-enzyme that, under anaerobic
conditions, is involved in dissimilation of glucose. The enzyme is also
present under aerobic conditions, its amount is about one-third and its
activity is only one-tenth of the values observed under anaerobic conditions.
Nevertheless, its function in the presence of oxygen remained ignored. The
data presented in this paper led us to propose that the enzyme has a
protective role against oxidative stress. Our results indicated that cells
deleted in adhE gene could not grow aerobically in minimal media,
were extremely sensitive to oxidative stress and showed division defects. In
addition, compared with wild type, mutant cells displayed increased levels of
internal peroxides (even higher than those found in a katG
strain) and increased protein carbonyl content. This pleiotropic phenotype
disappeared when the adhE gene was reintroduced into the defective
strain. The purified enzyme was highly reactive with hydrogen peroxide (with a
Ki of 5 µM), causing inactivation
due to a metal-catalyzed oxidation reaction. It is possible to prevent this
reactivity to hydrogen peroxide by zinc, which can replace the iron atom at
the catalytic site of AdhE. This can also be achieved by addition of
ZnSO4 to cell cultures. In such conditions, addition of hydrogen
peroxide resulted in reduced cell viability compared with that obtained
without the Zn treatment. We therefore propose that AdhE acts as a
H2O2 scavenger in Escherichia coli cells grown
under aerobic conditions.
Received for publication, April 25, 2003
, and in revised form, May 30, 2003.
* This work was funded by Grants BMC2001-0874 from Ministerio de Ciencia y
Tecnología (Spain) and 2000 SGR 0042 from Generalitat de Catalunya
(Spain). The costs of publication of this article were defrayed in part by the
payment of page charges. This article must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section 1734
solely to indicate this fact.
A recipient of a Ph.D. scholarship from the Ministerio de Educación
y Cultura (Spain).
To whom correspondence should be addressed: Dept. Ciències
Mèdiques Bàsiques, Facultat de Medicina, Av. Rovira Roure 44,
25198 Lleida, Spain. Tel.: 34-973-702-275; Fax: 34-973-702-426; E-mail:
joaquim.ros{at}cmb.udl.es.

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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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