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J. Biol. Chem., Vol. 281, Issue 15, 9845-9851, April 14, 2006

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The Carotenase AtCCD1 from Arabidopsis thaliana Is a Dioxygenase^*

Holger Schmidt¹, Robert Kurtzer, Wolfgang Eisenreich, and Wilfried Schwab

From the Foundation for Biomolecular Food Technology, Technische Universität München, Lise-Meitner-Strasse 34, D-84354 Freising, Germany and the Institute of Organic Chemistry and Biochemistry, Technische Universität München, Lichtenberg-Strasse 4, D-85747 Garching, Germany

Apocarotenoids resulting from the oxidative cleavage of carotenoids serve as important signaling and accessory molecules in a variety of biological processes. The enzymes catalyzing these reactions are referred to as carotenases or carotenoid oxygenases. Whether they act according to a monooxygenase mechanism, requiring two oxygens from different sources, or a dioxygenase mechanism is still a topic of controversy. In this study, we utilized the readily available -apo-8'-carotenal as a substrate for the heterologously expressed AtCCD1 protein from Arabidopsis thaliana to investigate the oxidative cleavage mechanism of the 9,10 double bond of carotenoids. -Ionone and a C₁₇-dialdehyde were detected as products by gas and liquid chromatography-mass spectrometry as well as NMR analysis. Labeling experiments using H₂¹⁸O or ¹⁸ O₂ showed that the oxygen in the keto-group of -ionone is derived solely from molecular dioxygen. When experiments were performed in an ¹⁸O₂-enriched atmosphere, a substantial fraction of the C₁₇-dialdehyde contained labeled oxygen. The results unambiguously demonstrate a dioxygenase mechanism for the carotenase AtCCD1 from A. thaliana.

Received for publication, October 28, 2005 , and in revised form, February 3, 2006.

^* This work was supported by the Federal Ministry for Economy and Technology of Germany via the AiF ZUTECH, Program 110 ZN. 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.

¹ To whom correspondence should be addressed. Tel.: 49-8161-548-320; Fax: 49-8161-548-595; E-mail: holger.schmidt{at}mytum.de.

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