Uphill energy transfer in photosystem I from Chlamydomonas reinhardtii. Time-resolved fluorescence measurements at 77 K View Full Text


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Article Info

DATE

2018-04-04

AUTHORS

Wojciech Giera, Sebastian Szewczyk, Michael D. McConnell, Kevin E. Redding, Rienk van Grondelle, Krzysztof Gibasiewicz

ABSTRACT

Energetic properties of chlorophylls in photosynthetic complexes are strongly modulated by their interaction with the protein matrix and by inter-pigment coupling. This spectral tuning is especially striking in photosystem I (PSI) complexes that contain low-energy chlorophylls emitting above 700 nm. Such low-energy chlorophylls have been observed in cyanobacterial PSI, algal and plant PSI–LHCI complexes, and individual light-harvesting complex I (LHCI) proteins. However, there has been no direct evidence of their presence in algal PSI core complexes lacking LHCI. In order to determine the lowest-energy states of chlorophylls and their dynamics in algal PSI antenna systems, we performed time-resolved fluorescence measurements at 77 K for PSI core and PSI–LHCI complexes isolated from the green alga Chlamydomonas reinhardtii. The pool of low-energy chlorophylls observed in PSI cores is generally smaller and less red-shifted than that observed in PSI–LHCI complexes. Excitation energy equilibration between bulk and low-energy chlorophylls in the PSI–LHCI complexes at 77 K leads to population of excited states that are less red-shifted (by ~ 12 nm) than at room temperature. On the other hand, analysis of the detection wavelength dependence of the effective trapping time of bulk excitations in the PSI core at 77 K provided evidence for an energy threshold at ~ 675 nm, above which trapping slows down. Based on these observations, we postulate that excitation energy transfer from bulk to low-energy chlorophylls and from bulk to reaction center chlorophylls are thermally activated uphill processes that likely occur via higher excitonic states of energy accepting chlorophylls. More... »

PAGES

321-335

References to SciGraph publications

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  • 2007-05. The structure of a plant photosystem I supercomplex at 3.4 Å resolution in NATURE
  • 2005-11. Spectral and Kinetic Analysis of the Energy Coupling in the PS I–LHC I Supercomplex from the Green Alga Chlamydomonas reinhardtii at 77 K in PHOTOSYNTHESIS RESEARCH
  • 2003-12. Crystal structure of plant photosystem I in NATURE
  • 2001-06. Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/s11120-018-0506-z

    DOI

    http://dx.doi.org/10.1007/s11120-018-0506-z

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/29619738


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    48 complex I protein
    49 complexes
    50 core
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    52 coupling
    53 cyanobacterial PSI
    54 dependence
    55 detection-wavelength dependence
    56 direct evidence
    57 dynamics
    58 effective trapping time
    59 energetic properties
    60 energy
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    62 energy threshold
    63 energy transfer
    64 equilibration
    65 evidence
    66 excitation
    67 excitation energy transfer
    68 excited states
    69 excitonic states
    70 fluorescence measurements
    71 green alga Chlamydomonas reinhardtii
    72 hand
    73 higher excitonic states
    74 interaction
    75 light-harvesting complex I (LHCI) proteins
    76 low-energy chlorophylls
    77 low-energy states
    78 matrix
    79 measurements
    80 observations
    81 order
    82 photosynthetic complexes
    83 photosystem I
    84 photosystem I (PSI) complexes
    85 pool
    86 population
    87 presence
    88 process
    89 properties
    90 protein
    91 protein matrix
    92 psi
    93 reaction center chlorophyll
    94 reinhardtii
    95 room temperature
    96 slow
    97 spectral tuning
    98 state
    99 system
    100 temperature
    101 threshold
    102 time
    103 time-resolved fluorescence measurements
    104 transfer
    105 trapping time
    106 tuning
    107 uphill energy transfer
    108 uphill process
    109 wavelength dependence
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