A method to decompose spectral changes in Synechocystis PCC 6803 during light-induced state transitions

A.M. Acuña, R. Kana, M.S. Gwizdala, J.J. Snellenburg, P. van Alphen, B.F. van Oort, D. Kirilovsky, R. van Grondelle, I.H.M. van Stokkum

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Cyanobacteria have developed responses to maintain the balance between the energy absorbed and the energy used in different pigment-protein complexes. One of the relatively rapid (a few minutes) responses is activated when the cells are exposed to high light intensities. This mechanism thermally dissipates excitation energy at the level of the phycobilisome (PB) antenna before it reaches the reaction center. When exposed to low intensities of light that modify the redox state of the plastoquinone pool, the so-called state transitions redistribute energy between photosystem I and II. Experimental techniques to investigate the underlying mechanisms of these responses, such as pulse-amplitude modulated fluorometry, are based on spectrally integrated signals. Previously, a spectrally resolved fluorometry method has been introduced to preserve spectral information. The analysis method introduced in this work allows to interpret SRF data in terms of species-associated spectra of open/closed reaction centers (RCs), (un)quenched PB and state 1 versus state 2. Thus, spectral differences in the time-dependent fluorescence signature of photosynthetic organisms under varying light conditions can be traced and assigned to functional emitting species leading to a number of interpretations of their molecular origins. In particular, we present evidence that state 1 and state 2 correspond to different states of the PB-PSII-PSI megacomplex.
Original languageEnglish
Pages (from-to)237-249
JournalPhotosynthesis Research
Volume130
Issue number1-3
DOIs
Publication statusPublished - 2016

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Phycobilisomes
Synechocystis
phycobilisome
Fluorometry
Plastoquinone
High intensity light
Photosystem I Protein Complex
Light
fluorometry
Photosystem II Protein Complex
Excitation energy
energy
Pigments
light intensity
Fluorescence
Cyanobacteria
Antennas
Oxidation-Reduction
photosystem I
autotrophs

Cite this

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title = "A method to decompose spectral changes in Synechocystis PCC 6803 during light-induced state transitions",
abstract = "Cyanobacteria have developed responses to maintain the balance between the energy absorbed and the energy used in different pigment-protein complexes. One of the relatively rapid (a few minutes) responses is activated when the cells are exposed to high light intensities. This mechanism thermally dissipates excitation energy at the level of the phycobilisome (PB) antenna before it reaches the reaction center. When exposed to low intensities of light that modify the redox state of the plastoquinone pool, the so-called state transitions redistribute energy between photosystem I and II. Experimental techniques to investigate the underlying mechanisms of these responses, such as pulse-amplitude modulated fluorometry, are based on spectrally integrated signals. Previously, a spectrally resolved fluorometry method has been introduced to preserve spectral information. The analysis method introduced in this work allows to interpret SRF data in terms of species-associated spectra of open/closed reaction centers (RCs), (un)quenched PB and state 1 versus state 2. Thus, spectral differences in the time-dependent fluorescence signature of photosynthetic organisms under varying light conditions can be traced and assigned to functional emitting species leading to a number of interpretations of their molecular origins. In particular, we present evidence that state 1 and state 2 correspond to different states of the PB-PSII-PSI megacomplex.",
author = "A.M. Acu{\~n}a and R. Kana and M.S. Gwizdala and J.J. Snellenburg and {van Alphen}, P. and {van Oort}, B.F. and D. Kirilovsky and {van Grondelle}, R. and {van Stokkum}, I.H.M.",
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A method to decompose spectral changes in Synechocystis PCC 6803 during light-induced state transitions. / Acuña, A.M.; Kana, R.; Gwizdala, M.S.; Snellenburg, J.J.; van Alphen, P.; van Oort, B.F.; Kirilovsky, D.; van Grondelle, R.; van Stokkum, I.H.M.

In: Photosynthesis Research, Vol. 130, No. 1-3, 2016, p. 237-249.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - A method to decompose spectral changes in Synechocystis PCC 6803 during light-induced state transitions

AU - Acuña, A.M.

AU - Kana, R.

AU - Gwizdala, M.S.

AU - Snellenburg, J.J.

AU - van Alphen, P.

AU - van Oort, B.F.

AU - Kirilovsky, D.

AU - van Grondelle, R.

AU - van Stokkum, I.H.M.

PY - 2016

Y1 - 2016

N2 - Cyanobacteria have developed responses to maintain the balance between the energy absorbed and the energy used in different pigment-protein complexes. One of the relatively rapid (a few minutes) responses is activated when the cells are exposed to high light intensities. This mechanism thermally dissipates excitation energy at the level of the phycobilisome (PB) antenna before it reaches the reaction center. When exposed to low intensities of light that modify the redox state of the plastoquinone pool, the so-called state transitions redistribute energy between photosystem I and II. Experimental techniques to investigate the underlying mechanisms of these responses, such as pulse-amplitude modulated fluorometry, are based on spectrally integrated signals. Previously, a spectrally resolved fluorometry method has been introduced to preserve spectral information. The analysis method introduced in this work allows to interpret SRF data in terms of species-associated spectra of open/closed reaction centers (RCs), (un)quenched PB and state 1 versus state 2. Thus, spectral differences in the time-dependent fluorescence signature of photosynthetic organisms under varying light conditions can be traced and assigned to functional emitting species leading to a number of interpretations of their molecular origins. In particular, we present evidence that state 1 and state 2 correspond to different states of the PB-PSII-PSI megacomplex.

AB - Cyanobacteria have developed responses to maintain the balance between the energy absorbed and the energy used in different pigment-protein complexes. One of the relatively rapid (a few minutes) responses is activated when the cells are exposed to high light intensities. This mechanism thermally dissipates excitation energy at the level of the phycobilisome (PB) antenna before it reaches the reaction center. When exposed to low intensities of light that modify the redox state of the plastoquinone pool, the so-called state transitions redistribute energy between photosystem I and II. Experimental techniques to investigate the underlying mechanisms of these responses, such as pulse-amplitude modulated fluorometry, are based on spectrally integrated signals. Previously, a spectrally resolved fluorometry method has been introduced to preserve spectral information. The analysis method introduced in this work allows to interpret SRF data in terms of species-associated spectra of open/closed reaction centers (RCs), (un)quenched PB and state 1 versus state 2. Thus, spectral differences in the time-dependent fluorescence signature of photosynthetic organisms under varying light conditions can be traced and assigned to functional emitting species leading to a number of interpretations of their molecular origins. In particular, we present evidence that state 1 and state 2 correspond to different states of the PB-PSII-PSI megacomplex.

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