Evidence map›Paper›PMID 41518050›Full record

ArticleThe FEBS journal2026

Phycocyanobilin biosynthesis in Galdieria sulphuraria requires isomerization of phycoerythrobilin synthesized by bilin reductases.

Federica Frascogna, Nathan C Rockwell, Jana Hartmann, Julie M Mudler, Nicole Frankenberg-Dinkel

Abstract read
In one paragraph

Article in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Federica FrascognaDepartment of Microbiology, RPTU University Kaiserslautern-Landau, Germany.
Nathan C RockwellDepartment of Molecular and Cellular Biology, University of California at Davis, CA, USA.
Jana HartmannDepartment of Microbiology, RPTU University Kaiserslautern-Landau, Germany.
Julie M MudlerDepartment of Microbiology, RPTU University Kaiserslautern-Landau, Germany.
Nicole Frankenberg-DinkelDepartment of Microbiology, RPTU University Kaiserslautern-Landau, Germany.ORCID 0000-0002-7757-6839

Funding

Basic Energy Sciences DE-SC0002395Deutsche Forschungsgemeinschaft FR1487/10-2
6 · The paper itself

Abstract

Phycobiliproteins are essential components of the light-harvesting antennae in cyanobacteria and red algae, requiring covalently bound open-chain tetrapyrrole chromophores (bilins) for proper function. In the red alga Galdieria sulphuraria, the primary chromophore is phycocyanobilin (PCB), despite the apparent presence of only biosynthetic genes for phycoerythrobilin (PEB) biosynthesis (PEBA and PEBB). This observation suggests the presence of an alternative, atypical biosynthetic pathway for PCB. In this study, we confirmed the presence of PEB:PCB isomerase activity in an enriched protein fraction from G. sulphuraria. To further investigate this unusual pathway, we combined in silico analyses with biochemical assays. Phylogenetic analyses confirmed the placement of the G. sulphuraria ferredoxin-dependent bilin reductases within the PEBA and PEBB lineages, typically associated with PEB synthesis, whereas the related red alga Cyanidioschyzon merolae was found to contain only PCYA. This gene distribution presents a functional paradox. G. sulphuraria harbors PEB biosynthesis genes but no detectable PEB chromophores and lacks known PCB-synthesizing enzymes despite containing PCB. Functional characterization of recombinant GsPEBA (G. sulphuraria PEBA) and GsPEBB (G. sulphuraria PEBB) confirmed their roles in PEB synthesis, demonstrating that these enzymes have not evolved to synthesize PCB or act as isomerases despite their phylogenetic placement. In contrast, CmPCYA (C. merolae PCYA) catalyzed direct PCB formation from biliverdin. Together, these findings reveal an atypical isomerase-based pathway for PCB biosynthesis in G. sulphuraria, expanding our understanding of bilin metabolism and providing new insight into the evolutionary flexibility of photosynthetic pigment biosynthesis in Rhodophyta.

Indexed as

OxidoreductasesPhycobilinsPhycocyaninRhodophytaAlgal ProteinsBile PigmentsIsomerismPhycoerythrinPhylogenyAlgal ProteinsBile PigmentsOxidoreductasesPhycobilinsPhycocyaninphycocyanobilinPhycoerythrinphycoerythrobilinlinear tetrapyrrolephycobilisomephycocyanobilinpigment biosynthesisrhodophytes

Identifiers

PMID41518050
PMCPMC13193486

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.