ArticleScientific reports2015
A biliverdin-binding cyanobacteriochrome from the chlorophyll d-bearing cyanobacterium Acaryochloris marina.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 102 citations in OpenAlex.
- Discovery and Engineering of Unique Cyanobacteriochrome GAF Domains.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Rotameric Heterogeneity of Conserved Tryptophan Is Responsible for Reduced Photochemical Quantum Yield in Cyanobacteriochrome Slr1393g3.Chemphyschem : a European journal of chemical physics and physical chemistry · 2025Article
- Cyanobacteriochromes: A Rainbow of Photoreceptors.Annual review of microbiology · 2024Review
- Red/green cyanobacteriochromes acquire isomerization from phycocyanobilin to phycoviolobilin.Protein science : a publication of the Protein Society · 2024Article
- Cyanobacteriochromes from Gloeobacterales Provide New Insight into the Diversification of Cyanobacterial Photoreceptors.Journal of molecular biology · 2024Article
- A Single-Site Mutation Tunes Fluorescence and Chromophorylation of an Orange Fluorescent Cyanobacteriochrome.Chembiochem : a European journal of chemical biology · 2023Article
- A Single Site Mutation Tunes Fluorescence and Chromophorylation of an Orange Fluorescent Cyanobacteriochrome.bioRxiv : the preprint server for biology · 2023Article
- Structure of proteins under pressure: Covalent binding effects of biliverdin on β-lactoglobulin.Biophysical journal · 2022Article
- A red-green photochromic bacterial protein as a new contrast agent for improved photoacoustic imaging.Photoacoustics · 2022Article
- Transition Metals Induce Quenching of Monomeric Near-Infrared Fluorescent Proteins.Biochemistry · 2022Article
- Protein-chromophore interactions controlling photoisomerization in red/green cyanobacteriochromes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Light- and pH-dependent structural changes in cyanobacteriochrome AnPixJg2.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Rapid directed molecular evolution of fluorescent proteins in mammalian cells.Protein science : a publication of the Protein Society · 2022Article
- Biliverdin incorporation into the cyanobacteriochrome SPI1085g3 fromFrontiers in microbiology · 2022Article
- Light-regulated gene expression in Bacteria: Fundamentals, advances, and perspectives.Frontiers in bioengineering and biotechnology · 2022Review
- The Red Edge: Bilin-Binding Photoreceptors as Optogenetic Tools and Fluorescence Reporters.Chemical reviews · 2021Review
- Identification of a dual orange/far-red and blue light photoreceptor from an oceanic green picoplankton.Nature communications · 2021Article
- c-di-GMP Homeostasis Is Critical for Heterocyst Development inFrontiers in microbiology · 2021Article
- A far-red cyanobacteriochrome lineage specific for verdins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Cruciality of Single Amino Acid Replacement for the Spectral Tuning of Biliverdin-Binding Cyanobacteriochromes.International journal of molecular sciences · 2020Article
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyanobacteriochromes (CBCRs) are linear tetrapyrrole-binding photoreceptors in cyanobacteria that absorb visible and near-ultraviolet light. CBCRs are divided into two types based on the type of chromophore they contain: phycocyanobilin (PCB) or phycoviolobilin (PVB). PCB-binding CBCRs reversibly photoconvert at relatively long wavelengths, i.e., the blue-to-red region, whereas PVB-binding CBCRs reversibly photoconvert at shorter wavelengths, i.e., the near-ultraviolet to green region. Notably, prior to this report, CBCRs containing biliverdin (BV), which absorbs at longer wavelengths than do PCB and PVB, have not been found. Herein, we report that the typical red/green CBCR AM1_1557 from the chlorophyll d-bearing cyanobacterium Acaryochloris marina can bind BV almost comparable to PCB. This BV-bound holoprotein reversibly photoconverts between a far red light-absorbing form (Pfr, λmax = 697 nm) and an orange light-absorbing form (Po, λmax = 622 nm). At room temperature, Pfr fluoresces with a maximum at 730 nm. These spectral features are red-shifted by 48~77 nm compared with those of the PCB-bound domain. Because the absorbance of chlorophyll d is red-shifted compared with that of chlorophyll a, the BV-bound AM1_1557 may be a physiologically relevant feature of A. marina and is potentially useful as an optogenetic switch and/or fluorescence imager.
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