Comparative Analysis of Ultrafast Excitation Energy-Transfer Pathways in Three Strains of Divinyl Chlorophyll a/b-Containing Cyanobacterium, Prochlorococcus marinus

Hamada, Fumiya; Murakami, Akio; Akimoto, Seiji

doi:10.1021/acs.jpcb.5b10073

Cited by 9 publications

(9 citation statements)

References 38 publications

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“…As described above, a pair of positive and negative peaks in the FDA spectrum is indicative of an energy transfer from a pigment with the positive peak to a pigment with the negative one. 40,41 When transition dipole moments with their strength are different between energy donors and accepters, magnitudes of the positive and negative peaks differ remarkably. Moreover, an S 1 −S 0 transition of Car is nearly forbidden, 2 and the moment of an S 1 −S 0 transition in Chl c is smaller than that of Chl a.…”

Section: ■ Discussionmentioning

confidence: 99%

“…Moreover, an S 1 −S 0 transition of Car is nearly forbidden, 2 and the moment of an S 1 −S 0 transition in Chl c is smaller than that of Chl a. 2 Therefore, only a negative peak is observed for Car→Chl a transfer, 41 whereas a pair of small positive and large negative peaks should be observed for Chl c→Chl a transfer. 31 It should be noted that a red-shifted Chl a, such as a low-energy Chl, has a larger transition dipole moment because of an exciton interaction.…”

Section: ■ Discussionmentioning

confidence: 99%

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Excitation-Energy Transfer and Quenching in Diatom PSI-FCPI upon P700 Cation Formation

et al. 2020

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Excitation-energy transfer in photosystem I (PSI) is changed by a cation formation of a special pair chlorophyll P700 in the PSI core; however, it remains unclear how light-harvesting pigment−protein complexes are involved in the P700-related energytransfer mechanisms. Here, we report effects of the redox changes of P700 on excitationenergy dynamics in diatom PSI-fucoxanthin chlorophyll a/c-binding protein (PSI-FCPI) and PSI core complexes by means of time-resolved fluorescence (TRF) spectroscopy. For the TRF measurements, the PSI-FCPI and PSI were adapted under P700 neutral and cation conditions using chemical reagents. Upon the P700 + formation, fluorescence decayassociated (FDA) spectra constructed from the TRF spectra exhibit a larger fluorescence decay amplitude relative to a fluorescence rise magnitude within 100 ps in each of the PSI-FCPI and PSI. The decay components are shifted to lower wavelengths in each of the P700cation PSI-FCPI and PSI than in the P700-neutral PSIs. The rapid fluorescence decays upon the P700 + formation are clearly verified by mean lifetimes reconstructed from the FDA spectra. Because the P700-cation PSI does not cause charge-separation reactions, the relatively strong decay components and rapid fluorescence decays observed are likely attributed to excitation-energy quenching. These observations suggest that chlorophylls in PSI and around/within FCPI are involved in the energy-quenching events by the redox changes of P700.

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Section: ■ Discussionmentioning

confidence: 99%

Section: ■ Discussionmentioning

confidence: 99%

Excitation-Energy Transfer and Quenching in Diatom PSI-FCPI upon P700 Cation Formation

et al. 2020

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“…12,22 The spectral profiles of the blue-LED-grown cells do not differ significantly from those of the white-light-grown cells. 11 In the red-LED-grown cells of CCMP1375 and CCMP2773, the relative absorbance of DV-Chl b is reduced compared with that of the blue-LED-grown cells. In the spectrum of the red-LEDgrown CCMP1375 cells, the intensity of the Soret band of DV-Chl b decreases, and another band appears on the shorterwavelength side.…”

Section: Methodsmentioning

confidence: 97%

“…In DV-Chl b-rich CCMP1375 and CCMP2773, not only DV-Chl b but also carotenoids (especially α-carotene) were significant energy donors to DV-Chl a. 11 The natural habitat of DV-Chl b-rich Prochlorococcus is located at the depths with only limited blue light. 12 Partensky et al investigated the effect of blue light, which peaks at 475 nm with a full width half-maximum (FWHM) of 100 nm, on DV-Chl b-rich CCMP1375 and DV-Chl a-rich CCMP1986.…”

Section: Introductionmentioning

confidence: 96%

Adaptation of Divinyl Chlorophyll a/b-Containing Cyanobacterium to Different Light Conditions: Three Strains of Prochlorococcus marinus

2017

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The light-harvesting mechanisms in the three strains of Prochlorococcus marinus, CCMP1986, CCMP1375, and CCMP2773, grown under blue and red light-emitting diodes (LEDs) at two intensity levels were investigated. The blue LED was divinyl chlorophyll b (DV-Chl b) selective and the red LED was DV-Chl a selective. Under the red LED, the relative amount of DV-Chl b in CCMP1375 and CCMP2773 decreased and the relative amount of zeaxanthin increased in CCMP1375. Furthermore, the pigment composition of cells of CCMP1375 grown under red LED was remodified when they were transplanted under the blue LED. Picosecond-time-resolved fluorescence of the LED-grown Prochlorococcus was measured, and the excitation-energy-transfer efficiency between DV-Chl a did not significantly change for the different LED colors or intensities; however, a change in the pigment composition of the DV-Chl b-rich strains (CCMP1375 and CCMP2773) was observed. It appears that peripheral antenna responds to light conditions, with small modifications in the photosystems.

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“…Fluorescence rise and decay curves at the femtosecond domain were measured with a fluorescence up-conversion system at 293 K (0.20 ps/channel) (67,68). The second harmonic (425 nm) of a Ti:Sapphire laser (Tsunami, Spectra-Physics, Mountain View, CA) was used as the excitation source, and its fundamental (850 nm) served as the gate pulse.…”

Section: Time-resolved Fluorescence Measurements and Analysismentioning

confidence: 99%

Fluorescence lifetime analyses reveal how the high light–responsive protein LHCSR3 transforms PSII light-harvesting complexes into an energy-dissipative state

Kim

Akimoto

Tokutsu

et al. 2017

Journal of Biological Chemistry

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In green algae, light-harvesting complex stress-related 3 (LHCSR3) is responsible for the pH-dependent dissipation of absorbed light energy, a function vital for survival under high-light conditions. LHCSR3 binds the photosystem II and light-harvesting complex II (PSII-LHCII) supercomplex and transforms it into an energy-dissipative form under acidic conditions, but the molecular mechanism remains unclear. Here we show that in the green alga , LHCSR3 modulates the excitation energy flow and dissipates the excitation energy within the light-harvesting complexes of the PSII supercomplex. Using fluorescence decay-associated spectra analysis, we found that, when the PSII supercomplex is associated with LHCSR3 under high-light conditions, excitation energy transfer from light-harvesting complexes to chlorophyll-binding protein CP43 is selectively inhibited compared with that to CP47, preventing excess excitation energy from overloading the reaction center. By analyzing femtosecond up-conversion fluorescence kinetics, we further found that pH- and LHCSR3-dependent quenching of the PSII-LHCII-LHCSR3 supercomplex is accompanied by a fluorescence emission centered at 684 nm, with a decay time constant of 18.6 ps, which is equivalent to the rise time constant of the lutein radical cation generated within a chlorophyll-lutein heterodimer. These results suggest a mechanism in which LHCSR3 transforms the PSII supercomplex into an energy-dissipative state and provide critical insight into the molecular events and characteristics in LHCSR3-dependent energy quenching.

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Comparative Analysis of Ultrafast Excitation Energy-Transfer Pathways in Three Strains of Divinyl Chlorophyll a/b-Containing Cyanobacterium, Prochlorococcus marinus

Cited by 9 publications

References 38 publications

Excitation-Energy Transfer and Quenching in Diatom PSI-FCPI upon P700 Cation Formation

Excitation-Energy Transfer and Quenching in Diatom PSI-FCPI upon P700 Cation Formation

Adaptation of Divinyl Chlorophyll a/b-Containing Cyanobacterium to Different Light Conditions: Three Strains of Prochlorococcus marinus

Fluorescence lifetime analyses reveal how the high light–responsive protein LHCSR3 transforms PSII light-harvesting complexes into an energy-dissipative state

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