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

Wolf-D. Woggon

doi:10.1351/pac200274081397

Publicly Available Published by De Gruyter January 1, 2009

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

Wolf-D. Woggon

From the journal Pure and Applied Chemistry

https://doi.org/10.1351/pac200274081397

Abstract

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 K_a > 106 mol_-1, which mimics the regiospecific enzymatic cleavage of carotenoids.

Conference

International Symposium on Carotenoids, International Symposium on Carotenoids, CAROT, Carotenoids, 13th, Honolulu, Hawaii, USA, 2002-01-06–2002-01-11

Published Online: 2009-01-01

Published in Print: 2002-01-01

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

Abstract

Conference

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