Ultrafast energy transfer dynamics of phycobilisome from Thermosynechococcus vulcanus, as revealed by ps fluorescence and fs pump-probe spectroscopies

Hirota, Yuma; Serikawa, Hiroki; Kawakami, Keisuke; Ueno, Masato; Kamiya, Nobuo; Kosumi, Daisuke

doi:10.1007/s11120-021-00844-0

Cited by 13 publications

(10 citation statements)

References 58 publications

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“…Because at the blue side, the amplitude of FDAS is positive with a maximum around 650 nm, while at the red side with no negative value (Figure 7a). Recently, Hirota et al also identified an EET pathway with a time of 7.3 ps in the PC rod [19]. The time component of 115 ps could be assigned to the time of EET from the PC rod to the APC core.…”

Section: Discussionmentioning

confidence: 99%

“…Womick et al showed a fast sub-picosecond EET component of 970 fs in the PC hexamer [17], Zhang et al found a time component of 18 ps which described an EET pathway from a terminal PC trimer to the APC core [18]. Recently, Hirota et al demonstrated the EET from the rod to the core and finally to the terminal emitter, taking place in a timescale from several ten picosecond seconds to nanoseconds within the PBS of Thermosynechococcus vulcanus by time-resolved fluorescence and pump-probe technique [19].…”

Section: Introductionmentioning

confidence: 99%

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Time-Resolved Fluorescence Spectroscopy Study of Energy Transfer Dynamics in Phycobilisomes from Cyanobacteria Thermosynechococcus vulcanus NIES 2134 and Synechocystis sp. PCC 6803

Xie

Xiao

et al. 2021

Crystals

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As the largest light-harvesting complex in cyanobacteria, phycobilisomes (PBSs) show high efficiency and a high rate of energy transfer, owing to an elegant antenna-like assembly. To understand the structural influence on the dynamic process of the energy transfer in PBSs, two cyanobacterium species Thermosynechococcus vulcanus NIES 2134 (T. 2134) and Synechocystis sp. PCC 6803 (S. 6803) with different rod–core-linked assemblies were chosen for this study. The dynamic process of the energy transfer in both PBSs was investigated through time-resolved fluorescence spectroscopy (TRFS) with a time resolution of sub-picosecond. Via the fluorescence decay curves deconvolution, the pathways and related rates of the excitation energy transfer (EET) were determined. Three time components, i.e., 10, 80, and 1250 ps, were identified in the EET in the PBSs of T. 2134 and three, i.e., 9, 115, and 1680 ps, in the EET in the PBSs of S. 6803. In addition, a comparison of the dynamic process of the energy transfer between the two cyanobacteria revealed how the PBS assembly affects the energy transfer in PBSs. The findings will provide insight into future time-resolved crystallography.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Time-Resolved Fluorescence Spectroscopy Study of Energy Transfer Dynamics in Phycobilisomes from Cyanobacteria Thermosynechococcus vulcanus NIES 2134 and Synechocystis sp. PCC 6803

Xie

Xiao

et al. 2021

Crystals

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“…Despite seemingly deleterious slow exciton hopping over the sparse arrangement of highly fluorescent chromophores, the complex maintains near-unity exciton transfer efficiency. , As detailed in numerous studies, the mechanisms yielding this high transfer efficiency are not well known. ,− Electron microscopy (EM) advances in recent years have elucidated the detailed structure of these megacomplexes and provided many clues about the underlying mechanisms. ,,− However, progress in resolving energy transfer dynamics using time-resolved spectroscopy has been slower owing to massive spectral congestion from hundreds of phycobilisome pigments. − Small energetic separations in the donor and acceptor chromophores in the network confound isolation of signal kinetics from individual pigments or complexes, hiding the principles driving high transfer efficiencies that operate on the supercomplex or quaternary level. An alternative to using spectral resolution to reveal excitonic pathways is to use the different dipole directions of the linear phycocyanobilin chromophores in the complex through polarization-dependent spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

Phycobilisome’s Exciton Transfer Efficiency Relies on an Energetic Funnel Driven by Chromophore–Linker Protein Interactions

Sohoni,

Lloyd,

Hitchcock

et al. 2023

J. Am. Chem. Soc.

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The phycobilisome is the primary light-harvesting antenna in cyanobacterial and red algal oxygenic photosynthesis. It maintains near-unity efficiency of energy transfer to reaction centers despite relying on slow exciton hopping along a relatively sparse network of highly fluorescent phycobilin chromophores. How the complex maintains this high efficiency remains unexplained. Using a two-dimensional electronic spectroscopy polarization scheme that enhances energy transfer features, we directly watch energy flow in the phycobilisome complex of Synechocystis sp. PCC 6803 from the outer phycocyanin rods to the allophycocyanin core. The observed downhill flow of energy, previously hidden within congested spectra, is faster than timescales predicted by Forster hopping along single rod chromophores. We attribute the fast, 8 ps energy transfer to interactions between rod-core linker proteins and terminal rod chromophores, which facilitate unidirectionally downhill energy flow to the core. This mechanism drives the high energy transfer efficiency in the phycobilisome and suggests that linker protein− chromophore interactions have likely evolved to shape its energetic landscape.

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“…Based on this structural model, they discovered a quick energy transfer pathway that took 888 fs to go from the rod to the core via linker proteins, and then 17 ps to get from the core to the terminal emitters (LCM) [16]. Then, using ps fluorescence and fs pump-probe spectroscopies, Kawakami et al discovered the energy transfer of 7.3 ps between PC trimers in rods, 53 ps from PC rod to APC core, and 180 ps in the APC core complex [17]. They also confirmed that the APC trimer, not the PC612 trimer, is located between the lower base core A cylinders and the higher B cylinder [18].…”

Section: Introductionmentioning

confidence: 99%

Ultrafast Energy Transfer Dynamics in a Cyanobacterial Light-Harvesting Phycobilisome

Xiao¹,

Guo²,

Liang³

et al. 2023

Preprint

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The phycobilisomes (PBS) of cyanobacteria and red algae are the primary light-harvesting an-tennas, absorbing solar energy and transporting it to photosynthetic reaction centres with ex-traordinary efficiency and rate. The mechanism of energy transfer in PBS should be investigated in conjunction with biological structural information, as the functions of proteins result from structures. Here, we report the energy transfer study in PBS from a thermophilic cyanobacte-rium Thermosynechococcus vulcanus NIES 2134 (T. 2134), with the Cryo-EM model resolved at near-atomic-resolution recently. The time-resolved fluorescence spectroscopy of PBS with the sub-picosecond resolution was discovered at 77K. Deconvolution of the fluorescence decay curve was then used to reveal the energy transfer channels and the associated transfer rates. Expert for the fluorescence lifetimes of terminal emitters, four time-components, i.e., 9 ps, 13 ps, 23 ps, and 55 ps, were recognised in the energy transfer in PBS. The energy transfer dynamics in PBS were further analysed by combining the cryo-EM structure and the spectral property. The findings aid our understanding of the energy transfer mechanisms in PBS.

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Ultrafast energy transfer dynamics of phycobilisome from Thermosynechococcus vulcanus, as revealed by ps fluorescence and fs pump-probe spectroscopies

Cited by 13 publications

References 58 publications

Time-Resolved Fluorescence Spectroscopy Study of Energy Transfer Dynamics in Phycobilisomes from Cyanobacteria Thermosynechococcus vulcanus NIES 2134 and Synechocystis sp. PCC 6803

Time-Resolved Fluorescence Spectroscopy Study of Energy Transfer Dynamics in Phycobilisomes from Cyanobacteria Thermosynechococcus vulcanus NIES 2134 and Synechocystis sp. PCC 6803

Phycobilisome’s Exciton Transfer Efficiency Relies on an Energetic Funnel Driven by Chromophore–Linker Protein Interactions

Ultrafast Energy Transfer Dynamics in a Cyanobacterial Light-Harvesting Phycobilisome

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