Identification of several sub-populations in the pool of light harvesting proteins in the pennate diatom Phaeodactylum tricornutum

Gundermann, Kathi; Schmidt, Matthias; Weisheit, Wolfram; Mittag, Maria; Büchel, Claudia

doi:10.1016/j.bbabio.2012.10.017

Cited by 74 publications

(62 citation statements)

References 35 publications

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“…reflecting the larger amount of fucoxanthin. Previous reports suggested that the FCP of P. tricornutum had a higher fucoxanthin/Chl a ratio than C. meneghiniana [36,37]. positive peak, and the lifetime was shorter than 300 ps, indicating quenching ability [15].…”

Section: Spectral Properties Of Fcp Complexes Isolated From Diatomsmentioning

confidence: 96%

Regulation of excitation energy transfer in diatom PSII dimer: How does it change the destination of excitation energy?

Yokono

Nagao

Tomo

et al. 2015

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Energy transfer dynamics in dimeric photosystem II (PSII) complexes isolated from four diatoms, Chaetoceros gracilis, Cyclotella meneghiniana, Thalassiosira pseudonana, and Phaeodactylum tricornutum, are examined. Time-resolved fluorescence measurements were conducted in the range of 0-80ns. Delayed fluorescence spectra showed a clear difference between PSII monomer and PSII dimer isolated from the four diatoms. The difference can be interpreted as reflecting suppressed energy transfer between PSII monomers in the PSII dimer for efficient energy trapping at the reaction center. The observation was especially prominent in C. gracilis and T. pseudonana. The pathways seem to be suppressed under a low pH condition in isolated PSII complexes from C. gracilis, and excitation energy may be quenched with fucoxanthin chlorophyll a/c-binding protein (FCP) that was closely associated with PSII in C. gracilis. The energy transfer between PSII monomers in the PSII dimer may play a role in excitation energy regulation in diatoms.

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Section: Spectral Properties Of Fcp Complexes Isolated From Diatomsmentioning

confidence: 96%

Regulation of excitation energy transfer in diatom PSII dimer: How does it change the destination of excitation energy?

Yokono

Nagao

Tomo

et al. 2015

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…The amount of Fcp6 depended on the light intensity during growth, as did the diatoxanthin content (Beer et al 2006 ). In contrast, in the pennate P. tricornutum , no Lhcx proteins could be found in trimeric complexes so far (Grouneva et al 2011 ;Gundermann et al 2013 ). Lepetit et al ( 2012 ) were the fi rst to propose that it is unlikely that Lhcx1 of P. tricornutum binds Dd or Dt, based on their interpretation of the work of Bailleul et al ( 2010 ).…”

Section: E Lhcx and Photoprotectionmentioning

confidence: 89%

“…Whereas the Lhcr and Lhcx proteins are very similar in centric and pennate diatoms, the Lhcf proteins fall into three different groups (Fig. 2.2 , adapted from Gundermann et al 2013 ), whereby two groups are more specifi c for pennates or centrics, respectively, and the third group contains members from both.…”

Section: A the Fucoxanthin-chlorophyll Proteinsmentioning

confidence: 98%

“…In LHCII, 8 Chl a , 6 Chl b and 4 carotenoids are bound per monomer (Liu et al 2004 ;Standfuss et al 2005 ). The pigment ratio of FCPs is around 3-4 Chl a : 1 Chl c : 3-4 Fx, depending on isolation procedure and species, whereby the FCPs of P. tricornutum are characterized by a higher amount of Fx (Beer et al 2006 ;Gundermann et al 2013 ;Joshi-Deo et al 2010 ;Lepetit et al 2007 ;Papagiannakis et al 2005 ). Because the Q Y absorption of FCPs is at a relatively short wavelength (671 nm, see Fig.…”

Section: Pigmentation Of Fucoxanthin-chlorophyll Proteinsmentioning

confidence: 98%

“…Diatom light-harvesting polypeptides can be differentiated into three groups, Lhcr, Lhcf and Lhcx proteins. Concerning pennate and centric diatoms, most of the Lhcf genes are different between the two groups as demonstrated by the phylogenetic tree (Adapted from Gundermann et al 2013 ) ( a , Phatr = P. tricornutum , Thaps = T. pseudonana ). All of them share the same topology with three membrane-spanning helices predicted to show the same arrangement as in LHCII, as depicted in the cartoon as side view into the membrane ( b ).…”

Section: B Supramolecular Organization Of Fucoxanthin-chlorophyll Prmentioning

confidence: 99%

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Structure and Functional Heterogeneity of Fucoxanthin-Chlorophyll Proteins in Diatoms

Gundermann

Büchel

2014

The Structural Basis of Biological Energy Generation

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SummaryFucoxanthin-chlorophyll proteins (FCPs) of diatoms are divided into three groups, the main light harvesting antennas Lhcf, the photosystem I-specifi c Lhcr, and Lhcx involved in photoprotection. All are closely related to higher plant light harvesting complexes (LHCs) when comparing sequences, albeit smaller and more hydrophobic. However, pigmentation differs from higher plant LHCs with around eight chlorophyll a , two chlorophyll c and six fucoxanthin per monomer. Fucoxanthin, with a carbonyl moiety conjugated to the polyene backbone, undergoes extreme bathochromic shifts upon protein binding, dividing the different fucoxanthins into more red, green and blue absorbing ones. Excitation energy transfer is extremely effi cient, either directly from chlorophyll c to chlorophyll a or from fucoxanthin to chlorophyll a involving the S 1 /ICT state of fucoxanthin. Most Lhcf assemble into trimers, whereby only in centric diatoms Lhcx was found in trimers as well, and specifi c oligomeric FCP complexes are present. Whereas the arrangement of FCPs around the photosystems is largely unknown, spectroscopic measurements together with homology considerations allow for a fi rst rough model of the pigment arrangement in trimeric and oligomeric FCP complexes. Blue fucoxanthin is bound analogously to lutein in LHCII, surrounded by the same four chlorophyll a , since binding sites are conserved. Additionally, chlorophyll a can be found in a604, a614, b605 and a611, although binding of the latter has to be different due to the lack of long wavelength absorption in FCPs. Chlorophyll c is most probably bound in b609 and a613. The red fucoxanthin cluster around helix 2, which has less sequence homology to LHCII. The green fucoxanthins are most probably located around the violaxanthin and b601 binding sites of LHCII, whereby the former is probably a mixed site for fucoxanthins and diadinoxanthin/diatoxanthin.

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Photosynthesis in Diatoms

Scarsini

Marchand

Manoylov

et al. 2019

Diatoms: Fundamentals and Applications

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Identification of several sub-populations in the pool of light harvesting proteins in the pennate diatom Phaeodactylum tricornutum

Cited by 74 publications

References 35 publications

Regulation of excitation energy transfer in diatom PSII dimer: How does it change the destination of excitation energy?

Regulation of excitation energy transfer in diatom PSII dimer: How does it change the destination of excitation energy?

Structure and Functional Heterogeneity of Fucoxanthin-Chlorophyll Proteins in Diatoms

Photosynthesis in Diatoms

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