NDLI: Excitation energy transfer from phycobiliprotein to chlorophyll d in intact cells of Acaryochloris marina studied by time- and wavelength-resolved fluorescence spectroscopy

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Photochemical & Photobiological Sciences Vol - 4 Issue - 9

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Excitation energy transfer from phycobiliprotein to chlorophyll d in intact cells of Acaryochloris marina studied by time- and wavelength-resolved fluorescence spectroscopy

Content Provider	Royal Society of Chemistry (RSC)
Author	Theiss, Christoph Kemnitz, Klaus Huyer, Joachim Larkum, Anthony Eckert, Hann-Jörg Schmitt, Franz-Josef Chen, Min Eichler, Hans Joachim Petrášek, Zdeněk
Copyright Year	2005
Abstract	The fluorescence decay spectra and the excitation energy transfer from the phycobiliproteins (PBP) to the chlorophyll-antennae of intact cells of the chlorophyll (Chl) d-dominated cyanobacterium Acaryochloris marina were investigated at 298 and 77 K by time- and wavelength-correlated single photon counting fluorescence spectroscopy. At 298 K it was found that (i) the fluorescence dynamics in A. marina is characterized by two emission peaks located at about 650 and 725 nm, (ii) the intensity of the 650 nm fluorescence depends strongly on the excitation wavelength, being high upon excitation of phycobiliprotein (PBP) at 632 nm but virtually absent upon excitation of chlorophyll at 430 nm, (iii) the 650 nm fluorescence band decayed predominantly with a lifetime of 70 ± 20 ps, (iv) the 725 nm fluorescence, which was observed independent of the excitation wavelength, can be described by a three-exponential decay kinetics with lifetimes depending on the open or the closed state (F0 or Fm) of the reaction centre of Photosystem II (PS II). Based on the results of this study, it is inferred that the excitation energy transfer from phycobiliproteins to Chl d of PS II in A. marina occurs with a time constant of about 70 ps, which is about three times faster than the energy transfer from the phycobilisomes to PS II in the Chl a-containing cyanobacterium Synechococcus 6301 (C. W. Mullineaux and A. R. Holzwarth, Biochim. Biophys. Acta, 1991, 68–78, 1098). A similar fast PBP to Chl d excitation energy transfer was also observed at 77 K. At 77 K a small long-lived fluorescence decay component with a lifetime of 14 ns was observed in the 640–700 nm spectral range. However, it has a rather featureless spectrum, not typical for Chl a, and was only observed upon excitation at 400 nm but not upon excitation at 632 and 654 nm. Thus, this long-lived fluorescence component cannot be used as an indicator that the primary PS II donor of Acaryochloris marina contains Chl a.
Starting Page	1016
Ending Page	1022
Page Count	7
File Format	HTM / HTML PDF
ISSN	1474905X
Volume Number	4
Issue Number	12
Journal	Photochemical & Photobiological Sciences
DOI	10.1039/b512350j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Subscribed
Subject Keyword	Absorption spectroscopy Photosynthetic reaction centre Chlorophyll Biochim Mullineaux Chl Synechococcus Fluorescence Photosystem II Holzwarth Phycobiliprotein Photon Wavelength Marina Acta Phycobilisome Cyanobacteria
Content Type	Text
Resource Type	Article
Subject	Physical and Theoretical Chemistry

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The nature of the photosystem II reaction centre in the chlorophyll d-containing prokaryote, Acaryochloris marina

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Photosystem trap energies and spectrally-dependent energy-storage efficiencies in the Chl d-utilizing cyanobacterium, Acaryochloris marina

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Time-resolved fluorescence emission measurements of photosystem I particles of various cyanobacteria: a unified compartmental model.

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Excitation energy transfer from phycobiliprotein to chlorophyll d in intact cells of Acaryochloris marina studied by time- and wavelength-resolved fluorescence spectroscopy

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The nature of the photosystem II reaction centre in the chlorophyll d-containing prokaryote, Acaryochloris marina

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Excitation energy transfer from phycobiliprotein to chlorophyll d in intact cells of Acaryochloris marina studied by time- and wavelength-resolved fluorescence spectroscopy