We are analyzing https://link.springer.com/article/10.1007/s11120-018-0576-y.

Title:
Biochemical characterization of photosystem I complexes having different subunit compositions of fucoxanthin chlorophyll a/c-binding proteins in the diatom Chaetoceros gracilis | Photosynthesis Research
Description:
Diatoms are dominant phytoplankton in aquatic environments and have unique light-harvesting apparatus, fucoxanthin chlorophyll a/c-binding protein (FCP). Diatom photosystem I (PSI) interacts with specific FCPs (FCPI); however, it remains unclear how PSI cores receive excitation energy from FCPI. To analyze the energy transfer dynamics, it is necessary to isolate both PSI cores and PSI–FCPI complexes. In this study, we prepared three PSI complexes, which are PSI–FCPI membrane fragments, detergent-solubilized PSI–FCPI supercomplexes and PSI core-like complexes, from the marine centric diatom, Chaetoceros gracilis, and examined their biochemical properties. Both the PSI–FCPI membrane fragments and supercomplexes showed similar subunit compositions including FCPI, whereas the PSI complexes were devoid of most FCPI subunits. The purity and homogeneity of the two detergent-solubilized PSI preparations were verified by clear-native PAGE and electron microscopy. The difference of pigment contents among the three PSI samples was shown by absorption spectra at 77 K. The intensity in the whole spectrum of PSI–FCPI membranes was much higher than those of the other two complexes, while the spectral shape of PSI complexes was similar to that of cyanobacterial PSI core complexes. 77-K fluorescence spectra of the three PSI preparations exhibited different spectral shapes, especially peak positions and band widths. Based on these observations, we discuss the merits of three PSI preparations for evaluating excitation energy dynamics in diatom PSI–FCPI complexes.
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Keywords {🔍}

article, pubmed, google, scholar, cas, photosystem, diatom, complexes, psi, biophys, chlorophyll, biochim, acta, nagao, science, fucoxanthin, proteins, chaetoceros, gracilis, akimoto, protein, characterization, suzuki, research, acbinding, energy, psifcpi, marine, access, supercomplex, complex, central, plant, photosynthesis, dohmae, shen, lightharvesting, japan, privacy, cookies, content, ueno, diatoms, excitation, transfer, centric, res, yokono, tomo, publish,

Topics {✒️}

n-dodecyl-β-d-maltoside chl detergent-solubilized psi–fcpi supercomplexes month download article/chapter diatom cyclotella meneghiniana time-resolved fluorescence spectroscopy oxygen-evolving thylakoid membranes monomeric photosystem i-complex plant psi-lhci supercomplex jian-ren shen diatom phaeodactylum tricornutum detergent-solubilized psi preparations psi–fcpi membrane fragments evolutionary cyanobacterial/algal intermediate expressing histidine-tagged subunits unique light-harvesting apparatus light-harvesting antenna proteins diatom psi–fcpi complexes specific fucoxanthin-chlorophyll protein fucoxanthin-chlorophyll-binding proteins diatom chaetoceros gracilis /c-binding protein complexes full article pdf photosystem ii supercomplex marine centric diatom light harvesting complex privacy choices/manage cookies psi–fcpi membranes article nagao light-harvesting chl light-harvesting ability light-harvesting strategy /c-binding protein author information authors /c-binding proteins trimeric fcp antennae structural basis free-living cyanobacterium fucoxanthin chlorophyll proteins fucoxanthin-chlorophyll proteins chlorophyll-carotenoid proteins light-harvesting complexes psi–fcpi complexes photosystem ii particles marine centric diatoms takehiro suzuki check access instant access psi preparations exhibited excitation energy relaxation thylakoid membrane proteome

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         headline:Biochemical characterization of photosystem I complexes having different subunit compositions of fucoxanthin chlorophyll a/c-binding proteins in the diatom Chaetoceros gracilis
         description:Diatoms are dominant phytoplankton in aquatic environments and have unique light-harvesting apparatus, fucoxanthin chlorophyll a/c-binding protein (FCP). Diatom photosystem I (PSI) interacts with specific FCPs (FCPI); however, it remains unclear how PSI cores receive excitation energy from FCPI. To analyze the energy transfer dynamics, it is necessary to isolate both PSI cores and PSI–FCPI complexes. In this study, we prepared three PSI complexes, which are PSI–FCPI membrane fragments, detergent-solubilized PSI–FCPI supercomplexes and PSI core-like complexes, from the marine centric diatom, Chaetoceros gracilis, and examined their biochemical properties. Both the PSI–FCPI membrane fragments and supercomplexes showed similar subunit compositions including FCPI, whereas the PSI complexes were devoid of most FCPI subunits. The purity and homogeneity of the two detergent-solubilized PSI preparations were verified by clear-native PAGE and electron microscopy. The difference of pigment contents among the three PSI samples was shown by absorption spectra at 77 K. The intensity in the whole spectrum of PSI–FCPI membranes was much higher than those of the other two complexes, while the spectral shape of PSI complexes was similar to that of cyanobacterial PSI core complexes. 77-K fluorescence spectra of the three PSI preparations exhibited different spectral shapes, especially peak positions and band widths. Based on these observations, we discuss the merits of three PSI preparations for evaluating excitation energy dynamics in diatom PSI–FCPI complexes.
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      description:Diatoms are dominant phytoplankton in aquatic environments and have unique light-harvesting apparatus, fucoxanthin chlorophyll a/c-binding protein (FCP). Diatom photosystem I (PSI) interacts with specific FCPs (FCPI); however, it remains unclear how PSI cores receive excitation energy from FCPI. To analyze the energy transfer dynamics, it is necessary to isolate both PSI cores and PSI–FCPI complexes. In this study, we prepared three PSI complexes, which are PSI–FCPI membrane fragments, detergent-solubilized PSI–FCPI supercomplexes and PSI core-like complexes, from the marine centric diatom, Chaetoceros gracilis, and examined their biochemical properties. Both the PSI–FCPI membrane fragments and supercomplexes showed similar subunit compositions including FCPI, whereas the PSI complexes were devoid of most FCPI subunits. The purity and homogeneity of the two detergent-solubilized PSI preparations were verified by clear-native PAGE and electron microscopy. The difference of pigment contents among the three PSI samples was shown by absorption spectra at 77 K. The intensity in the whole spectrum of PSI–FCPI membranes was much higher than those of the other two complexes, while the spectral shape of PSI complexes was similar to that of cyanobacterial PSI core complexes. 77-K fluorescence spectra of the three PSI preparations exhibited different spectral shapes, especially peak positions and band widths. Based on these observations, we discuss the merits of three PSI preparations for evaluating excitation energy dynamics in diatom PSI–FCPI complexes.
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