ArticleThe Journal of biological chemistry2009
Phycourobilin in trichromatic phycocyanin from oceanic cyanobacteria is formed post-translationally by a phycoerythrobilin lyase-isomerase.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 90 citations in OpenAlex.
- Improved Stability and Brightness Following Iterative Redesign of a De Novo Biliprotein.Biochemistry · 2026Article
- Genomic analysis highlights a novel class of DPCF-type cyanobacteriochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026Article
- Red Seaweed-Derived Phycobiliproteins: Marine Bioactive Colorants with Functional Health Properties.Marine drugs · 2026Review
- Phycocyanobilin biosynthesis in Galdieria sulphuraria requires isomerization of phycoerythrobilin synthesized by bilin reductases.The FEBS journal · 2026Article
- Phycoerythrin from algae: functional properties, bioactivities, production challenges, and industrial prospects.Archives of microbiology · 2026Review
- Natural color biofactories: advancing the spectrum of pigment production in phototrophic microbes.FEMS microbes · 2025Review
- The Unique Light-Harvesting System of the Algal Phycobilisome: Structure, Assembly Components, and Functions.International journal of molecular sciences · 2023Review
- Phycobilisomes and Phycobiliproteins in the Pigment Apparatus of Oxygenic Photosynthetics: From Cyanobacteria to Tertiary Endosymbiosis.International journal of molecular sciences · 2023Review
- Diversity and Evolution of Pigment Types in Marine Synechococcus Cyanobacteria.Genome biology and evolution · 2022Article
- Crystal structure and molecular mechanism of an E/F type bilin lyase-isomerase.Structure (London, England : 1993) · 2022Article
- Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives.Computational and structural biotechnology journal · 2022Review
- The Red Edge: Bilin-Binding Photoreceptors as Optogenetic Tools and Fluorescence Reporters.Chemical reviews · 2021Review
- Molecular bases of an alternative dual-enzyme system for light color acclimation of marineProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Chromophorylation of a Novel Cyanobacteriochrome GAF Domain fromJournal of microbiology and biotechnology · 2021Article
- Spectroscopic and Photophysical Investigation of Model Dipyrroles Common to Bilins: Exploring Natural Design for Steering Torsion to Divergent Functions.Frontiers in chemistry · 2021Article
- Effects of Cadmium on Bioaccumulation, Bioabsorption, and Photosynthesis inInternational journal of environmental research and public health · 2020Article
- Interplay between differentially expressed enzymes contributes to light color acclimation in marineProceedings of the National Academy of Sciences of the United States of America · 2019Article
- CpeF is the bilin lyase that ligates the doubly linked phycoerythrobilin on β-phycoerythrin in the cyanobacteriumThe Journal of biological chemistry · 2019Article
- Fluorescence Properties of a Novel Cyanobacteriochrome GAF Domain fromInternational journal of molecular sciences · 2018Article
- Biosynthesis of Fluorescent β Subunits of C-Phycocyanin fromMolecules (Basel, Switzerland) · 2018Article
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Authors and funding
13 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most cyanobacteria harvest light with large antenna complexes called phycobilisomes. The diversity of their constituting phycobiliproteins contributes to optimize the photosynthetic capacity of these microorganisms. Phycobiliprotein biosynthesis, which involves several post-translational modifications including covalent attachment of the linear tetrapyrrole chromophores (phycobilins) to apoproteins, begins to be well understood. However, the biosynthetic pathway to the blue-green-absorbing phycourobilin (lambda(max) approximately 495 nm) remained unknown, although it is the major phycobilin of cyanobacteria living in oceanic areas where blue light penetrates deeply into the water column. We describe a unique trichromatic phycocyanin, R-PC V, extracted from phycobilisomes of Synechococcus sp. strain WH8102. It is evolutionarily remarkable as the only chromoprotein known so far that absorbs the whole wavelength range between 450 and 650 nm. R-PC V carries a phycourobilin chromophore on its alpha-subunit, and this can be considered an extreme case of adaptation to blue-green light. We also discovered the enzyme, RpcG, responsible for its biosynthesis. This monomeric enzyme catalyzes binding of the green-absorbing phycoerythrobilin at cysteine 84 with concomitant isomerization to phycourobilin. This reaction is analogous to formation of the orange-absorbing phycoviolobilin from the red-absorbing phycocyanobilin that is catalyzed by the lyase-isomerase PecE/F in some freshwater cyanobacteria. The fusion protein, RpcG, and the heterodimeric PecE/F are mutually interchangeable in a heterologous expression system in Escherichia coli. The novel R-PC V likely optimizes rod-core energy transfer in phycobilisomes and thereby adaptation of a major phytoplankton group to the blue-green light prevailing in oceanic waters.
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