ArticlePhotochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology2025
FeSBCP analogue from cyanobacteria: insights from in vitro and in silico studies.
Article in Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
The blue light responsive Cryptochrome/Photolyase Family harbours two important photoactivatable proteins - cryptochromes and photolyases. While cryptochromes are essentially photoreceptors with diverse biological activities including circadian rhythm, photolyases repair UV damaged cyclobutane pyrimidine dimers (CPD) or (6-4) pyrimidine-pyrimidone photoadducts. Both cryptochromes and photolyases share a common Photolyase Homology Region (PHR) where they harbour a light harvesting antenna chromophore and redox-active flavin di-nucleotide (FAD). Even though photolyases do not possess an extension in the C-terminal region unlike cryptochromes, a recent discovery of FeS cluster containing bacterial cryptochrome-photolyase proteins (FeSBCPs) present an interesting retreat from the conventional photolyase architecture. They possess an additional modular redox center, [4Fe4S] iron-sulfur cluster connected by conserved cysteine residues. Herein, we characterize a cyanobacterial FeSBCP from Cyanobium sp. (CyPhrB) using tools from bioinformatics, biochemistry and biophysics. Sequence analysis reveals substitution in the well-conserved aromatic residues, meant for electron transfer. In silico modeling and docking supported by electrophoretic mobility shift assay as well as spectroscopic measurements do suggest efficient binding and repair of CyPhrB to damaged single/double-stranded substrates containing 6 -4 <TT> photolesion. Considering FeS clusters' established roles in DNA binding/repair activities, we speculate the role of FeS clusters in FeSBCPs and existence of FeS-FAD-DNA triangle towards efficient electron transfer.
Indexed as
Identifiers
41247631What OpenQuestion holds
Registered trials
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.