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J. Biol. Chem., Vol. 278, Issue 22, 19891-19897, May 30, 2003

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Characterization of YqjM, an Old Yellow Enzyme Homolog from Bacillus subtilis Involved in the Oxidative Stress Response^*

Teresa B. Fitzpatrick , Nikolaus Amrhein and Peter Macheroux 

From the ETH-Zürich, Institut für Pflanzenwissenschaften, Universitätstrasse 2, CH-8092 Zürich, Switzerland

In this paper, we demonstrate that a protein from Bacillus subtilis (YqjM) shares many characteristic biochemical properties with the homologous yeast Old Yellow Enzyme (OYE); the enzyme binds FMN tightly but noncovalently, preferentially uses NADPH as a source of reducing equivalents, and forms charge transfer complexes with phenolic compounds such as p-hydroxybenzaldehyde. Like yeast OYE and other members of the family, YqjM catalyzes the reduction of the double bond of an array of ,-unsaturated aldehydes and ketones including nitroester and nitroaromatic compounds. Although yeast OYE was the first member of this family to be discovered in 1933 and was the first flavoenzyme ever to be isolated, the physiological role of the family still remains obscure. The finding that ,-unsaturated compounds are substrates provoked speculation that the OYE family might be involved in reductive degradation of xenobiotics or lipid peroxidation products. Here, for the first time, we demonstrate on the protein level that whereas YqjM shows a basal level of expression in B. subtilis, the addition of the toxic xenobiotic, trinitrotoluene, leads to a rapid induction of the protein in vivo denoting a role in detoxification. Moreover, we show that YqjM is rapidly induced in response to oxidative stress as exerted by hydrogen peroxide, demonstrating a potential physiological role for this enigmatic class of proteins.

Received for publication, November 19, 2002 , and in revised form, February 7, 2003.

This work is dedicated to the late Prof. Vincent Massey (deceased August 26, 2002), a pioneer of enzymology who shaped flavoprotein research for over 40 years.

^* This project was executed as an offspin of a project supported by the Swiss National Science Foundation (to N. A. and P. M.). 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.

Present address: International University of Bremen, School of Engineering and Science, Campus Ring 6, D-28759 Bremen, Germany.

To whom correspondence may be addressed. Tel.: 41-1-6323841; Fax: 41-1-6321044; E-mail: teresa.fitzpatrick{at}ipw.biol.elhz.ch.

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