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Pure and Applied Chemistry

The Scientific Journal of IUPAC

Ed. by Burrows, Hugh / Weir, Ron / Stohner, Jürgen

12 Issues per year


IMPACT FACTOR 2013: 3.112
Rank 41 out of 148 in category Multidisciplinary Chemistry in the 2013 Thomson Reuters Journal Citation Report/Science Edition

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Oxidative cleavage of carotenoids catalyzed by enzyme models and beta-carotene 15,15´-monooxygenase

Wolf-D. Woggon1

1Institute of Organic Chemistry, University of Basel, St. Johanns-Ring 19, CH-4056 Basel, Switzerland

Citation Information: Pure and Applied Chemistry. Volume 74, Issue 8, Pages 1397–1408, ISSN (Online) 1365-3075, ISSN (Print) 0033-4545, DOI: 10.1351/pac200274081397, January 2009

Publication History

Published Online:
2009-01-01

The enzyme that catalyzes the central cleavage of β-carotene is an iron monooxygenase. The protein was isolated from chicken intestinal mucosa and overexpressed in two different cell lines. Inductively coupled plasma (ICP) emission analysis revealed that the hydrophobic 60.3-kDa enzyme contains one iron/mole protein. The substrate specificity was investigated, and the reaction mechanism elucidated incubating α-carotene in the presence of highly enriched 17O2 and H218O. A supramolecular enzyme model was synthesized, binding carotenoids Ka > 106 mol-1, which mimics the regiospecific enzymatic cleavage of carotenoids.

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