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Cited by 118Light effects on plantsPhotosynthetic Processes and MechanismsNeonatal Health and Biochemistry

The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.

Inactivation of phytochrome- and phycobiliprotein-chromophore precursors by rat liver biliverdin reductase

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Terry, M J, Maines, M D, Lagarias, J C·1993·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)74286-0
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Abstract

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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Metadata

Authors
Terry, M. J., Maines, M. D., & Lagarias, J. C.
Affiliations
  • University of Rochester Medicine (US)
  • University of California, Davis (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1993-12
Volume
268
Issue
35
Pages
26099-26106
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)74286-0
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
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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