Fluorescence from low-energy chlorophylls in Photosystem I of Synechocystis sp. PCC 6803 at physiological temperatures

Bruce P. Wittmershaus, Trung D. Tran, Brittny Panaia

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Fluorescence spectra from Photosystem I (PS I) are measured from 25 to -5°C on a PS II-less mutant of the cyanobacterium Synechocystis sp. PCC 6803. Emission from antenna chlorophylls (Chls) with energy levels below that of the reaction center, or low-energy Chls (LE Chls), is resolved verifying their presence at physiological temperatures. The 25°C spectrum is characterized by peaks at 688 and 715 nm. As temperature decreases, fluorescence at 688 nm decreases while at 715 nm it increases. The total fluorescence yield does not change. The temperature dependent spectra are fit to a sum of two basis spectra. At 25°C, the first basis spectrum has a major peak at 686 nm and a minor peak at 740 nm. This is attributed to fluorescence from the majority or bulk antenna Chls. The second basis spectrum has a major peak at 712 nm, with shoulders at 722 and 770 nm. It characterizes fluorescence from a small number of LE Chls. A progressive shift to the red in the fluorescence spectra occurs as the temperature is decreased. The temperature dependence in the relative amount of fluorescence from the bulk and LE Chls is fit using a two-component energy transfer model at thermal equilibrium.

Original languageEnglish (US)
Pages (from-to)29-39
Number of pages11
JournalPhotosynthesis research
Volume57
Issue number1
DOIs
StatePublished - Jan 1 1998

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Synechocystis sp. PCC 6803
Synechocystis
Photosystem I Protein Complex
photosystem I
Chlorophyll
Fluorescence
fluorescence
chlorophyll
Temperature
energy
temperature
light harvesting complex
Antennas
Energy Transfer
Cyanobacteria
energy transfer
shoulders
Energy transfer
Electron energy levels
Hot Temperature

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Plant Science
  • Cell Biology

Cite this

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title = "Fluorescence from low-energy chlorophylls in Photosystem I of Synechocystis sp. PCC 6803 at physiological temperatures",
abstract = "Fluorescence spectra from Photosystem I (PS I) are measured from 25 to -5°C on a PS II-less mutant of the cyanobacterium Synechocystis sp. PCC 6803. Emission from antenna chlorophylls (Chls) with energy levels below that of the reaction center, or low-energy Chls (LE Chls), is resolved verifying their presence at physiological temperatures. The 25°C spectrum is characterized by peaks at 688 and 715 nm. As temperature decreases, fluorescence at 688 nm decreases while at 715 nm it increases. The total fluorescence yield does not change. The temperature dependent spectra are fit to a sum of two basis spectra. At 25°C, the first basis spectrum has a major peak at 686 nm and a minor peak at 740 nm. This is attributed to fluorescence from the majority or bulk antenna Chls. The second basis spectrum has a major peak at 712 nm, with shoulders at 722 and 770 nm. It characterizes fluorescence from a small number of LE Chls. A progressive shift to the red in the fluorescence spectra occurs as the temperature is decreased. The temperature dependence in the relative amount of fluorescence from the bulk and LE Chls is fit using a two-component energy transfer model at thermal equilibrium.",
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Fluorescence from low-energy chlorophylls in Photosystem I of Synechocystis sp. PCC 6803 at physiological temperatures. / Wittmershaus, Bruce P.; Tran, Trung D.; Panaia, Brittny.

In: Photosynthesis research, Vol. 57, No. 1, 01.01.1998, p. 29-39.

Research output: Contribution to journalArticle

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AU - Wittmershaus, Bruce P.

AU - Tran, Trung D.

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N2 - Fluorescence spectra from Photosystem I (PS I) are measured from 25 to -5°C on a PS II-less mutant of the cyanobacterium Synechocystis sp. PCC 6803. Emission from antenna chlorophylls (Chls) with energy levels below that of the reaction center, or low-energy Chls (LE Chls), is resolved verifying their presence at physiological temperatures. The 25°C spectrum is characterized by peaks at 688 and 715 nm. As temperature decreases, fluorescence at 688 nm decreases while at 715 nm it increases. The total fluorescence yield does not change. The temperature dependent spectra are fit to a sum of two basis spectra. At 25°C, the first basis spectrum has a major peak at 686 nm and a minor peak at 740 nm. This is attributed to fluorescence from the majority or bulk antenna Chls. The second basis spectrum has a major peak at 712 nm, with shoulders at 722 and 770 nm. It characterizes fluorescence from a small number of LE Chls. A progressive shift to the red in the fluorescence spectra occurs as the temperature is decreased. The temperature dependence in the relative amount of fluorescence from the bulk and LE Chls is fit using a two-component energy transfer model at thermal equilibrium.

AB - Fluorescence spectra from Photosystem I (PS I) are measured from 25 to -5°C on a PS II-less mutant of the cyanobacterium Synechocystis sp. PCC 6803. Emission from antenna chlorophylls (Chls) with energy levels below that of the reaction center, or low-energy Chls (LE Chls), is resolved verifying their presence at physiological temperatures. The 25°C spectrum is characterized by peaks at 688 and 715 nm. As temperature decreases, fluorescence at 688 nm decreases while at 715 nm it increases. The total fluorescence yield does not change. The temperature dependent spectra are fit to a sum of two basis spectra. At 25°C, the first basis spectrum has a major peak at 686 nm and a minor peak at 740 nm. This is attributed to fluorescence from the majority or bulk antenna Chls. The second basis spectrum has a major peak at 712 nm, with shoulders at 722 and 770 nm. It characterizes fluorescence from a small number of LE Chls. A progressive shift to the red in the fluorescence spectra occurs as the temperature is decreased. The temperature dependence in the relative amount of fluorescence from the bulk and LE Chls is fit using a two-component energy transfer model at thermal equilibrium.

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