Immunocytochemical localization of photosystem I and the fucoxanthin-chlorophylla/c light-harvesting complex in the diatomPhaeodactylum tricornutum

Pyszniak, Andrew M.; Gibbs, Sarah P.

doi:10.1007/bf01322783

Cited by 108 publications

(70 citation statements)

References 30 publications

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“…(NPQ at this site furthermore depends on the presence of the de-epoxidized xanthophyll cycle pigment Dtx.) The heterogeneous lipid distribution in the thylakoid membranes of diatoms also supports the existence of different FCP pools and macrodomains of the pigment-protein complexes [33], although no variability of stacked to exposed membranes is observed by electron microscopy [34].…”

Section: Resultsmentioning

confidence: 53%

Functional heterogeneity of the fucoxanthins and fucoxanthin-chlorophyll proteins in diatom cells revealed by their electrochromic response and fluorescence and linear dichroism spectra

Szabó¹,

Premvardhan²,

Lepetit³

et al. 2010

Chemical Physics

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In this work, by analyzing the electrochromic transient spectra, the 77 K fluorescence emission and excitation, as well as the linear dichroism (LD) and circular dichroism (CD) spectra of low-light (LL) and high-light (HL) grown Phaeodactylum tricornutum cells, we show that the fucoxanthins (Fx) and fucoxanthin-chlorophyll proteins (FCP) exhibit marked functional heterogeneity. Electrochromic transients reveal that LL and HL cells differ substantially in their relative contents of two Fx forms, which absorb at 501 and 550 nm; they exhibit distinct LD signals but are CD silent. Fluorescence emission and excitation spectra at 77K reveal that although both forms efficiently transfer excitation energy to Chl a, the red form feeds somewhat more energy to photosystem II than to photosystem I. Similar data obtained in Cyclotella meneghiniana cells suggest that the heterogeneity of the FCP pool, with different Fx, forms plays a role in the regulation of energy utilization in FCP-containing organisms.

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Section: Resultsmentioning

confidence: 53%

Functional heterogeneity of the fucoxanthins and fucoxanthin-chlorophyll proteins in diatom cells revealed by their electrochromic response and fluorescence and linear dichroism spectra

Szabó¹,

Premvardhan²,

Lepetit³

et al. 2010

Chemical Physics

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“…[47] In contrast to higher plants, bacillariophyta show no distinction between stroma and grana thylakoids and the thylakoid membranes are arranged in stack of three. [48][49] [50] Also the antenna systems are entirely different between species: there are cyanobacterial phycobilisomes, membrane integral fucaxanthin enriched fucoxanthin chlorophyll a/c binding proteins (FCPs) of the diatoms and brown algae as well as light-harvesting complexes II (LHCIIs) of green algae and higher plants (for a recent review see [51]). In diatoms also the silicate cell walls vary extremely in their architectures.…”

Section: Introductionmentioning

confidence: 99%

Photo-CIDNP in the Reaction Center of the Diatom Cyclotella meneghiniana Observed by ¹³C MAS NMR

Zill

Kansy

Goss

et al. 2016

Zeitschrift Für Physikalische Chemie

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Photo-CIDNP in the reaction center of the diatom Cyclotella meneghiniana observed by 13 C MAS NMRThe solid-state photo-CIDNP effect in a new kingdom of the tree of life Abstract: Photo-CIDNP MAS NMR presents a unique tool to obtain insight into the photosynthetic reaction centers (RCs) of bacteria and plants. Using the dramatic enhancement of sensitivity and selectivity of the solid-state photo-CIDNP effect, structural as well as functional information can be obtained from the cofactor molecules forming a light-induced spin-correlated radical pair (SCRP) in a given reaction center. Here we demonstrate that the effect can be observed in a further species, which belongs neither to the plant nor the bacteria kingdom. Cyclotella (C.) meneghiniana is a member of the diatom phylum and, therefore, belongs to the kingdom of chromista. Chromista are some of the most productive organisms in nature, even in comparison to trees and terrestrial grasses. The observation of the effect in chromista indicates that the effect occurs in all photosynthetic organisms and completes the list with the last phototrophic kingdoms. Our data also demonstrate that the photo-and spin-chemical machineries of photosystem I of plants and chromista are very similar with respect to structure as well as function.

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“…In diatoms, the photosynthetic apparatus organization di¡ers in many respects from that of higher plants. The thylakoids are loosely appressed and organized in extended bands of three without grana stacking and PS I and II are not segregated [2]. The lightharvesting complexes (LHCs), which contain chlorophyll (Chl) a, Chl c, fucoxanthin and the xanthophyll cycle pigments [3], are equally distributed among appressed and nonappressed regions [2] and there is no evidence of any state transitions [4].…”

Section: Introductionmentioning

confidence: 99%

In diatoms, a transthylakoid proton gradient alone is not sufficient to induce a non‐photochemical fluorescence quenching

2002

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Non-photochemical £uorescence quenching (NPQ) in diatoms is associated with a xanthophyll cycle involving diadinoxanthin (DD) and its de-epoxidized form, diatoxanthin (DT). In higher plants, an obligatory role of de-epoxidized xanthophylls in NPQ remains controversial and the presence of a transthylakoid proton gradient (v vpH) alone may induce NPQ. We used inhibitors to alter the amplitude of v vpH and/or DD de-epoxidation, and coupled NPQ. No v vpH-dependent quenching was detected in the absence of DT. In diatoms, both v vpH and DT are required for NPQ. The binding of DT to protonated antenna sites could be obligatory for energy dissipation. ß

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Immunocytochemical localization of photosystem I and the fucoxanthin-chlorophylla/c light-harvesting complex in the diatomPhaeodactylum tricornutum

Cited by 108 publications

References 30 publications

Functional heterogeneity of the fucoxanthins and fucoxanthin-chlorophyll proteins in diatom cells revealed by their electrochromic response and fluorescence and linear dichroism spectra

Functional heterogeneity of the fucoxanthins and fucoxanthin-chlorophyll proteins in diatom cells revealed by their electrochromic response and fluorescence and linear dichroism spectra

Photo-CIDNP in the Reaction Center of the Diatom Cyclotella meneghiniana Observed by ¹³C MAS NMR

In diatoms, a transthylakoid proton gradient alone is not sufficient to induce a non‐photochemical fluorescence quenching

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Immunocytochemical localization of photosystem I and the fucoxanthin-chlorophylla/c light-harvesting complex in the diatomPhaeodactylum tricornutum

Cited by 108 publications

References 30 publications

Functional heterogeneity of the fucoxanthins and fucoxanthin-chlorophyll proteins in diatom cells revealed by their electrochromic response and fluorescence and linear dichroism spectra

Functional heterogeneity of the fucoxanthins and fucoxanthin-chlorophyll proteins in diatom cells revealed by their electrochromic response and fluorescence and linear dichroism spectra

Photo-CIDNP in the Reaction Center of the Diatom Cyclotella meneghiniana Observed by 13C MAS NMR

In diatoms, a transthylakoid proton gradient alone is not sufficient to induce a non‐photochemical fluorescence quenching

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Photo-CIDNP in the Reaction Center of the Diatom Cyclotella meneghiniana Observed by ¹³C MAS NMR