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Appl. Chem. Vol. 74, No. 8, pp.
Pure and Applied
Vol. 74, Issue 8
Oxidative cleavage of carotenoids catalyzed by enzyme models
and beta-carotene 15,15´-monooxygenase*
Institute of Organic Chemistry, University of Basel,
St. Johanns-Ring 19, CH-4056 Basel, Switzerland
Abstract: The enzyme that catalyzes the central cleavage
of b-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 a-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.
*Lecture presented at the 13 th International Symposium
on Carotenoids, Honolulu, Hawaii, USA, 6-11 January 2002.
Other lectures are published in this issue, pp. 1369-1477.
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