ArticleThe Journal of biological chemistry2014
Analysis of carotenoid isomerase activity in a prototypical carotenoid cleavage enzyme, apocarotenoid oxygenase (ACO).
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- Spectroscopy and crystallography define carotenoid oxygenases as a new subclass of mononuclear non-heme FeThe Journal of biological chemistry · 2025Article
- Preparation of carotenoid cleavage dioxygenases for X-ray crystallography.Methods in enzymology · 2022Article
- Article
- Rational Alteration of Pharmacokinetics of Chiral Fluorinated and Deuterated Derivatives of Emixustat for Retinal Therapy.Journal of medicinal chemistry · 2021Article
- The Structural and Biochemical Basis of Apocarotenoid Processing by β-Carotene Oxygenase-2.ACS chemical biology · 2021Article
- Molecular components affecting ocular carotenoid and retinoid homeostasis.Progress in retinal and eye research · 2021Review
- Structural and mechanistic aspects of carotenoid cleavage dioxygenases (CCDs).Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Evolutionary aspects and enzymology of metazoan carotenoid cleavage oxygenases.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- Structural basis for carotenoid cleavage by an archaeal carotenoid dioxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Evidence for distinct rate-limiting steps in the cleavage of alkenes by carotenoid cleavage dioxygenases.The Journal of biological chemistry · 2019Article
- Preparation and characterization of metal-substituted carotenoid cleavage oxygenases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Insights into the pathogenesis of dominant retinitis pigmentosa associated with a D477G mutation in RPE65.Human molecular genetics · 2018Article
- Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center.Biochemistry · 2017Article
- Synthesis and reactivity of a 4His enzyme model complex.RSC advances · 2017Article
- Structure and mechanism of NOV1, a resveratrol-cleaving dioxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Key Residues for Catalytic Function and Metal Coordination in a Carotenoid Cleavage Dioxygenase.The Journal of biological chemistry · 2016Article
- Utilization of Dioxygen by Carotenoid Cleavage Oxygenases.The Journal of biological chemistry · 2015Article
- Characterization of the Role of β-Carotene 9,10-Dioxygenase in Macular Pigment Metabolism.The Journal of biological chemistry · 2015Article
- Catalytic mechanism of a retinoid isomerase essential for vertebrate vision.Nature chemical biology · 2015Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Carotenoid cleavage enzymes (CCEs) constitute a group of evolutionarily related proteins that metabolize a variety of carotenoid and non-carotenoid substrates. Typically, these enzymes utilize a non-heme iron center to oxidatively cleave a carbon-carbon double bond of a carotenoid substrate. Some members also isomerize specific double bonds in their substrates to yield cis-apocarotenoid products. The apocarotenoid oxygenase from Synechocystis has been hypothesized to represent one such member of this latter category of CCEs. Here, we developed a novel expression and purification protocol that enabled production of soluble, native ACO in quantities sufficient for high resolution structural and spectroscopic investigation of its catalytic mechanism. High performance liquid chromatography and Raman spectroscopy revealed that ACO exclusively formed all-trans products. We also found that linear polyoxyethylene detergents previously used for ACO crystallization strongly inhibited the apocarotenoid oxygenase activity of the enzyme. We crystallized the native enzyme in the absence of apocarotenoid substrate and found electron density in the active site that was similar in appearance to the density previously attributed to a di-cis-apocarotenoid intermediate. Our results clearly demonstrated that ACO is in fact a non-isomerizing member of the CCE family. These results indicate that careful selection of detergent is critical for the success of structural studies aimed at elucidating structures of CCE-carotenoid/retinoid complexes.
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