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Inactivation of phytochrome- and phycobiliprotein-chromophore precursors by rat liver biliverdin reductase
Open accessAbstract
The phytochrome chromophore precursor, 3E-phytochromobilin, and the phycobiliprotein chromophore precursors, 3E-phycocyanobilin and 3E-phycoerythrobilin, are enzymatically converted to novel rubinoid products by purified rat liver biliverdin reductase. Phytochromobilin and phycocyanobilin are particularly good substrates for biliverdin reductase with Km and Vmax values very similar to those of the natural substrate, biliverdin IX alpha. Phycoerythrobilin is the least preferred of the three bilin substrates. 1H NMR spectroscopy of phycocyanorubin, the product of phycocyanobilin catalysis by biliverdin reductase, and comparison of absorption spectra of all three rubinoid products reveal that the C10 methine bridge is selectively reduced by biliverdin reductase without altering the A-ring ethylidene substituent. In vitro phytochrome assembly experiments demonstrate that the phytorubin products do not form photoactive adducts with recombinant apophytochrome. These results suggest that ectopic expression of biliverdin reductase in plants will prevent assembly of the functional photoreceptor and thus will potentially alter light-mediated plant growth and development.
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“Thus, by suppressing adipocyte oxidative stress, spirulina may lead to systemic anti-inflammatory and insulin-sensitising effects.12–20”
From Effects of spirulina on weight loss and blood lipids: A review (2020) · cites this paper as [12]
In the citing paper
“Phycocyanobilin is structurally similar to bilirubin and can inhibit NADPH oxidase.”
From Effects of spirulina on weight loss and blood lipids: A review (2020) · cites this paper as [12]
In the citing paper
“The antioxidant activity of spirulina has been proven to be directly proportional to the quantity of phycocyanin (which contains phycocyanobilin).12–14 45”
From Effects of spirulina on weight loss and blood lipids: A review (2020) · cites this paper as [12]
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Metadata
- Authors
- Terry, M. J., Maines, M. D., & Lagarias, J. C.
- Affiliations
- University of Rochester Medicine (US)
- University of California, Davis (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1993-12
- Volume
- 268
- Issue
- 35
- Pages
- 26099-26106
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1553174726
- Cited by
- 118
- References
- 39
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 6 · 2023: 5 · 2022: 4 · 2021: 10 · 2020: 7 · 2019: 2 · 2018: 3 · 2017: 4 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 3 · 2012: 5
- FWCI
- 1.96
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ePrints Soton (University of Southampton) (submittedVersion, cc-by)
- Funders
- National Institute of Environmental Health Sciences (ES04066, R01ES004066)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Health Sciences › Medicine › Pediatrics, Perinatology and Child Health › Neonatal Health and Biochemistry
- Keywords
- biliverdin reductase, phytochrome, phycobiliproteins, phytochromobilin, phycocyanobilin, phycoerythrobilin, rat liver
- MeSH terms
- Animals, Apoproteins, Biliverdine, Catalysis, Liver, Oxidoreductases, Phycocyanin, Phycoerythrin, Phytochrome, Plants, Pyrroles, Substrate Specificity, Oxidoreductases Acting on CH-CH Group Donors, Tetrapyrroles, Rats, Phycobilins, Eukaryota
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