Evidence map›Paper›PMID 38224422›Full record

ArticlePhotosynthesis research2024

Spectral and conformational characteristics of phycocyanin associated with changes of medium pH.

E Yu Parshina, W Liu, A I Yusipovich, D A Gvozdev, Y He, S K Pirutin, E A Klimanova, E G Maksimov, G V Maksimov

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Article in Photosynthesis research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

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0cells of the map it votes in
3citing papers in PubMed
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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

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

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4 · The record

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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

9 authors.

E Yu ParshinaFaculty of Biology, Shenzhen MSU-BIT University, Shenzhen, 518172, China. parshinae@gmail.com.
W LiuFaculty of Biology, Shenzhen MSU-BIT University, Shenzhen, 518172, China.
A I YusipovichFaculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991.
D A GvozdevFaculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991.
Y HeFaculty of Biology, Shenzhen MSU-BIT University, Shenzhen, 518172, China.
S K PirutinFaculty of Biology, Shenzhen MSU-BIT University, Shenzhen, 518172, China.
E A KlimanovaFaculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991.
E G MaksimovFaculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991.
G V MaksimovFaculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991.

Funding

Russian Science Foundation 21-44-00005
6 · The paper itself

Abstract

C-phycocyanin (C-PC) is the main component of water-soluble light-harvesting complexes (phycobilisomes, PBS) of cyanobacteria. PBS are involved in the absorption of quantum energy and the transfer of electronic excitation energy to the photosystems. A specific environment of C-PC chromophoric groups is provided by the protein matrix structure including protein-protein contacts between different subunits. Registration of C-PC spectral characteristics and the fluorescence anisotropy decay have revealed a significant pH influence on the chromophore microenvironment: at pH 5.0, a chromophore is more significantly interacts with the solvent, whereas at pH 9.0 the chromophore microenvironment becomes more viscous. Conformations of chromophores and the C-PC protein matrix have been studied by Raman and infrared spectroscopy. A decrease in the medium pH results in changes in the secondary structure either the C-PC apoproteins and chromophores, the last one adopts a more folded conformation.

Indexed as

Bacterial ProteinsLight-Harvesting Protein ComplexesPhycocyaninSpirulinaFluorescence PolarizationHydrogen-Ion ConcentrationProtein FoldingProtein Structure, SecondarySpectrophotometry, InfraredSpectrum Analysis, RamanBacterial ProteinsLight-Harvesting Protein ComplexesPhycocyaninC-phycocyanin (C-PC)Fluorescence anisotropy decayInfrared (IR) spectroscopyRaman spectroscopy

Identifiers

PMID38224422

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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.