ArticleProceedings of the National Academy of Sciences of the United States of America2006
Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXalpha, a key enzyme in the biosynthesis of phycocyanobilin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. 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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20 citing papers in PubMed, 77 citations in OpenAlex.
- Evolutionary insights into bilin biosynthesis: Functional characterization of pre-PcyA enzymes.Protein science : a publication of the Protein Society · 2026Article
- Phycocyanobilin biosynthesis in Galdieria sulphuraria requires isomerization of phycoerythrobilin synthesized by bilin reductases.The FEBS journal · 2026Article
- Engineering of Phycourobilin Synthase: PubS to a Two-Electron Reductase.Plant & cell physiology · 2025Article
- Rational Design of Key Enzymes to Efficiently Synthesize Phycocyanobilin inBiomolecules · 2024Article
- Elucidating the origins of phycocyanobilin biosynthesis and phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Crystal structure of a far-red-sensing cyanobacteriochrome reveals an atypical bilin conformation and spectral tuning mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome.The Journal of biological chemistry · 2020Article
- Crystal structure of the first eukaryotic bilin reductaseThe Journal of biological chemistry · 2019Article
- Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Ferredoxin-dependent bilin reductases in eukaryotic algae: Ubiquity and diversity.Journal of plant physiology · 2017Article
- The phycocyanobilin chromophore of streptophyte algal phytochromes is synthesized by HY2.The New phytologist · 2017Article
- Insights into the biosynthesis and assembly of cryptophycean phycobiliproteins.The Journal of biological chemistry · 2014Article
- Expression, purification and preliminary X-ray crystallographic analysis of cyanobacterial biliverdin reductase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Biliverdin amides reveal roles for propionate side chains in bilin reductase recognition and in holophytochrome assembly and photoconversion.Biochemistry · 2010Article
- Structural basis for hydration dynamics in radical stabilization of bilin reductase mutants.Biochemistry · 2010Article
- Electrostatic interaction of phytochromobilin synthase and ferredoxin for biosynthesis of phytochrome chromophore.The Journal of biological chemistry · 2010Article
- Structural insights into vinyl reduction regiospecificity of phycocyanobilin:ferredoxin oxidoreductase (PcyA).The Journal of biological chemistry · 2010Article
- Structure of the biliverdin radical intermediate in phycocyanobilin:ferredoxin oxidoreductase identified by high-field EPR and DFT.Journal of the American Chemical Society · 2009Article
- Flexible mapping of homology onto structure with homolmapper.BMC bioinformatics · 2007Article
- Diversity and evolution of phycobilisomes in marine Synechococcus spp.: a comparative genomics study.Genome biology · 2007Article
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4 authors at 2 institutions in 1 country.
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Abstract
Phytobilins (light harvesting and photoreceptor pigments in higher plants, algae, and cyanobacteria) are synthesized from biliverdin IXalpha (BV) by ferredoxin-dependent bilin reductases (FDBRs). Phycocyanobilin:ferredoxin oxidoreductase (PcyA), one such FDBR, is a new class of radical enzymes that require neither cofactors nor metals and serially reduces the vinyl group of the D-ring and A-ring of BV using four electrons from ferredoxin to produce phycocyanobilin, one of the phytobilins. We have determined the crystal structure of PcyA from Synechocystis sp. PCC 6803 in complex with BV, revealing the first tertiary structure of an FDBR family member. PcyA is folded in a three-layer alpha/beta/alpha sandwich structure, in which BV in a cyclic conformation is positioned between the beta-sheet and C-terminal alpha-helices. The basic patch on the PcyA surface near the BV molecule may provide a binding site for acidic ferredoxin, allowing direct transfer of electrons to BV. The orientation of BV is definitely fixed in PcyA by several hydrophilic interactions and the shape of the BV binding pocket of PcyA. We propose the mechanism by which the sequential reduction of the D- and A-rings is controlled, where Asp-105, located between the two reduction sites, would play the central role by changing its conformation during the reaction. Homology modeling of other FDBRs based on the PcyA structure fits well with previous genetic and biochemical data, thereby providing a structural basis for the reaction mechanism of FDBRs.
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