Non-a chlorophylls in cyanobacteria

Averina, Svetlana; Величко, Н. В.; Пиневич, А. А.; Senatskaya, Ekaterina; Pinevich, Alexander V.

doi:10.32615/ps.2019.130

Cited by 13 publications

(7 citation statements)

References 107 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Few known Prochlorophyta members form three genera, namely, Prochlorococcus, Prochloron, and Prochlorothrix, with cells having green or greenish color. The genus Prochlorothrix is represented by two filamentous freshwater species, P. hollandica [30] and P. scandica [31]. P. didemni, the only one known species of the Prochloron genus, is an obligate symbiont of the didemnid ascidia Lissoclinum patella [32].…”

Section: Prochlorophyta: Chlorophyll B-containing Cyanobacteriamentioning

confidence: 99%

Phycobilisomes and Phycobiliproteins in the Pigment Apparatus of Oxygenic Photosynthetics: From Cyanobacteria to Tertiary Endosymbiosis

Stadnichuk

Kusnetsov

2023

IJMS

View full text Add to dashboard Cite

Eukaryotic photosynthesis originated in the course of evolution as a result of the uptake of some unstored cyanobacterium and its transformation to chloroplasts by an ancestral heterotrophic eukaryotic cell. The pigment apparatus of Archaeplastida and other algal phyla that emerged later turned out to be arranged in the same way. Pigment-protein complexes of photosystem I (PS I) and photosystem II (PS II) are characterized by uniform structures, while the light-harvesting antennae have undergone a series of changes. The phycobilisome (PBS) antenna present in cyanobacteria was replaced by Chl a/b- or Chl a/c-containing pigment–protein complexes in most groups of photosynthetics. In the form of PBS or phycobiliprotein aggregates, it was inherited by members of Cyanophyta, Cryptophyta, red algae, and photosynthetic amoebae. Supramolecular organization and architectural modifications of phycobiliprotein antennae in various algal phyla in line with the endosymbiotic theory of chloroplast origin are the subject of this review.

show abstract

Section: Prochlorophyta: Chlorophyll B-containing Cyanobacteriamentioning

confidence: 99%

Phycobilisomes and Phycobiliproteins in the Pigment Apparatus of Oxygenic Photosynthetics: From Cyanobacteria to Tertiary Endosymbiosis

Stadnichuk

Kusnetsov

2023

IJMS

View full text Add to dashboard Cite

show abstract

“…In the majority of cyanobacteria, Chl a represents the only chlorophyll while in rare cases other chlorophylls are additionally produced [4,5].…”

Section: Photosynthetic Apparatus In Cyanobacteriamentioning

confidence: 99%

Far-Red Light Absorbing Photosynthetic Pigments in Cyanobacteria: Steady-State Fluorescence Detection, Time-Resolved Fluorescence Spectroscopy, and Confocal Laser Scanning Microscopy

Averina¹,

Senatskaya²,

Пиневич³

2020

Fluorescence Methods for Investigation of Living Cells and Microorganisms

View full text Add to dashboard Cite

The use of far-red light (FRL) is observed in some cyanobacteria, as well as in some marine and freshwater algae. While algae mobilize FRL absorbing antenna, which contains common chlorophyll a (Chl a), cyanobacteria produce red-shifted Chl d and/or Chl f. These pigments are synthesized either irrespective of ambient light or synthesized during FRL photoacclimation (FaRLiP), or adaptive remodeling of photosynthetic apparatus induced by relative enrichment with FRL quanta. The presence of red-shifted chlorophylls as well as their functions and topography are registered with various methods based on fluorescence measurement, such as: (1) steady-state fluorescence detection in live cells, cell fractions, and photosynthetic apparatus constituents; (2) time-resolved fluorescence spectroscopy, which traces energy transfer between individual pigments; (3) confocal laser scanning microscopy (CLSM), which helps to localize photosynthetic pigments in situ. This chapter describes photosynthetic apparatus in cyanobacteria and their photoacclimation phenomena. Over past decades, FRL photoacclimation has been studied in a small number of cyanobacteria. Novel Chl f-producing strains Chlorogloeopsis sp. CALU 759 and Synechocystis sp. CALU 1173 would represent promising model objects. Importantly, although they belong to alternative morphotypes and distant phylogenetic lineages, fluorescence pattern of their FRL-grown cells similarly falls within general FaRLiP response.

show abstract

“…Chl f has a 2-formyl in the C2-position of Chl a responsible for bulk red-shifted absorption and possesses the most red-shifted absorption in chlorophylls [ 20 ]. Chl f enables cyanobacteria to utilize habitats in low white light (WL) and high FRL conditions [ 21 , 22 , 23 , 24 , 25 , 26 ]. Far-red light acclimation is also reported in endolithic cyanobacteria [ 22 , 27 , 28 ].…”

Section: Introductionmentioning

confidence: 99%

“…Chl f is detected in isolated PSI and PSII systems induced by FRL conditions in the following Chl f -producing cyanobacteria: Chroococcidiopsis thermalis , Synechococcus sp. PCC 7335, and Halomicronema hongdechloris [ 19 , 29 , 30 , 31 , 32 ], although quite a few other cyanobacteria have been reported to produce Chl f [ 22 , 23 , 24 , 25 , 26 ]. Absorption spectra of naturally occurring Chl f -containing photosystems are more red-shifted than those of heterologously produced Chl f -containing PS complexes, owing to a relatively higher Chl f content [ 29 , 32 ].…”

Section: Introductionmentioning

confidence: 99%

Modeling the Characteristic Residues of Chlorophyll f Synthase (ChlF) from Halomicronema hongdechloris to Determine Its Reaction Mechanism

Chen,

Sawicki,

Wang

2023

Microorganisms

View full text Add to dashboard Cite

Photosystem II (PSII) is a quinone-utilizing photosynthetic system that converts light energy into chemical energy and catalyzes water splitting. PsbA (D1) and PsbD (D2) are the core subunits of the reaction center that provide most of the ligands to redox-active cofactors and exhibit photooxidoreductase activities that convert quinone and water into quinol and dioxygen. The performed analysis explored the putative uncoupled electron transfer pathways surrounding P680+ induced by far-red light (FRL) based on photosystem II (PSII) complexes containing substituted D1 subunits in Halomicronema hongdechloris. Chlorophyll f-synthase (ChlF) is a D1 protein paralog. Modeling PSII-ChlF complexes determined several key protein motifs of ChlF. The PSII complexes included a dysfunctional Mn4CaO5 cluster where ChlF replaced the D1 protein. We propose the mechanism of chlorophyll f synthesis from chlorophyll a via free radical chemistry in an oxygenated environment created by over-excited pheophytin a and an inactive water splitting reaction owing to an uncoupled Mn4CaO5 cluster in PSII-ChlF complexes. The role of ChlF in the formation of an inactive PSII reaction center is under debate, and putative mechanisms of chlorophyll f biosynthesis are discussed.

show abstract

Non-a chlorophylls in cyanobacteria

Cited by 13 publications

References 107 publications

Phycobilisomes and Phycobiliproteins in the Pigment Apparatus of Oxygenic Photosynthetics: From Cyanobacteria to Tertiary Endosymbiosis

Phycobilisomes and Phycobiliproteins in the Pigment Apparatus of Oxygenic Photosynthetics: From Cyanobacteria to Tertiary Endosymbiosis

Far-Red Light Absorbing Photosynthetic Pigments in Cyanobacteria: Steady-State Fluorescence Detection, Time-Resolved Fluorescence Spectroscopy, and Confocal Laser Scanning Microscopy

Modeling the Characteristic Residues of Chlorophyll f Synthase (ChlF) from Halomicronema hongdechloris to Determine Its Reaction Mechanism

Contact Info

Product

Resources

About