Energy transfer from chlorophyll f to the trapping center in naturally occurring and engineered Photosystem I complexes

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Abstract

Certain cyanobacteria can thrive in environments enriched in far-red light (700–800 nm) due to an acclimation process known as far-red light photoacclimation (FaRLiP). During FaRLiP, about 8% of the Chl a molecules in the photosystems are replaced by Chl f and a very small amount of Chl d. We investigated the spectroscopic properties of Photosystem I (PSI) complexes isolated from wild-type (WT) Synechococcus sp. PCC 7335 and a chlF mutant strain (lacking Chl f synthase) grown in white and far-red light (WL–PSI and FRL–PSI, respectively). WT–FRL–PSI complexes contain Chl f and Chl a but not Chl d. The light-minus dark difference spectrum of the trapping center at high spectral resolution indicates that the special pair in WT–FRL–PSI consists of Chl a molecules with maximum bleaching at 703–704 nm. The action spectrum for photobleaching of the special pair showed that Chl f molecules absorbing at wavelengths up to 800 nm efficiently transfer energy to the trapping center in FRL–PSI complexes to produce a charge-separated state. This is ~ 50 nm further into the near IR than WL–PSI; Chl f has a quantum yield equivalent to that of Chl a in the antenna, i.e., ~ 1.0. PSI complexes from Synechococcus 7002 carrying 3.8 Chl f molecules could promote photobleaching of the special pair by energy transfer at wavelengths longer than WT PSI complexes. Results from these latter studies are directly relevant to the issue of whether introduction of Chl f synthase into plants could expand the wavelength range available for oxygenic photosynthesis in crop plants.

Original languageEnglish (US)
Pages (from-to)151-163
Number of pages13
JournalPhotosynthesis research
Volume141
Issue number2
DOIs
StatePublished - Aug 15 2019

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Photosystem I Protein Complex
far-red light
Energy Transfer
photosystem I
energy transfer
Energy transfer
trapping
chlorophyll
wavelengths
Light
photobleaching
Synechococcus
Photobleaching
Molecules
Wavelength
bleaching
antennae
Photosynthesis
Acclimatization
Spectral resolution

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Plant Science
  • Cell Biology

Cite this

@article{e43bc5bf47d4441bb0865de3895716f9,
title = "Energy transfer from chlorophyll f to the trapping center in naturally occurring and engineered Photosystem I complexes",
abstract = "Certain cyanobacteria can thrive in environments enriched in far-red light (700–800 nm) due to an acclimation process known as far-red light photoacclimation (FaRLiP). During FaRLiP, about 8{\%} of the Chl a molecules in the photosystems are replaced by Chl f and a very small amount of Chl d. We investigated the spectroscopic properties of Photosystem I (PSI) complexes isolated from wild-type (WT) Synechococcus sp. PCC 7335 and a chlF mutant strain (lacking Chl f synthase) grown in white and far-red light (WL–PSI and FRL–PSI, respectively). WT–FRL–PSI complexes contain Chl f and Chl a but not Chl d. The light-minus dark difference spectrum of the trapping center at high spectral resolution indicates that the special pair in WT–FRL–PSI consists of Chl a molecules with maximum bleaching at 703–704 nm. The action spectrum for photobleaching of the special pair showed that Chl f molecules absorbing at wavelengths up to 800 nm efficiently transfer energy to the trapping center in FRL–PSI complexes to produce a charge-separated state. This is ~ 50 nm further into the near IR than WL–PSI; Chl f has a quantum yield equivalent to that of Chl a in the antenna, i.e., ~ 1.0. PSI complexes from Synechococcus 7002 carrying 3.8 Chl f molecules could promote photobleaching of the special pair by energy transfer at wavelengths longer than WT PSI complexes. Results from these latter studies are directly relevant to the issue of whether introduction of Chl f synthase into plants could expand the wavelength range available for oxygenic photosynthesis in crop plants.",
author = "Vasily Kurashov and Ho, {Ming Yang} and Gaozhong Shen and Karla Piedl and Laremore, {Tatiana N.} and Bryant, {Donald A.} and Golbeck, {John H.}",
year = "2019",
month = "8",
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language = "English (US)",
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TY - JOUR

T1 - Energy transfer from chlorophyll f to the trapping center in naturally occurring and engineered Photosystem I complexes

AU - Kurashov, Vasily

AU - Ho, Ming Yang

AU - Shen, Gaozhong

AU - Piedl, Karla

AU - Laremore, Tatiana N.

AU - Bryant, Donald A.

AU - Golbeck, John H.

PY - 2019/8/15

Y1 - 2019/8/15

N2 - Certain cyanobacteria can thrive in environments enriched in far-red light (700–800 nm) due to an acclimation process known as far-red light photoacclimation (FaRLiP). During FaRLiP, about 8% of the Chl a molecules in the photosystems are replaced by Chl f and a very small amount of Chl d. We investigated the spectroscopic properties of Photosystem I (PSI) complexes isolated from wild-type (WT) Synechococcus sp. PCC 7335 and a chlF mutant strain (lacking Chl f synthase) grown in white and far-red light (WL–PSI and FRL–PSI, respectively). WT–FRL–PSI complexes contain Chl f and Chl a but not Chl d. The light-minus dark difference spectrum of the trapping center at high spectral resolution indicates that the special pair in WT–FRL–PSI consists of Chl a molecules with maximum bleaching at 703–704 nm. The action spectrum for photobleaching of the special pair showed that Chl f molecules absorbing at wavelengths up to 800 nm efficiently transfer energy to the trapping center in FRL–PSI complexes to produce a charge-separated state. This is ~ 50 nm further into the near IR than WL–PSI; Chl f has a quantum yield equivalent to that of Chl a in the antenna, i.e., ~ 1.0. PSI complexes from Synechococcus 7002 carrying 3.8 Chl f molecules could promote photobleaching of the special pair by energy transfer at wavelengths longer than WT PSI complexes. Results from these latter studies are directly relevant to the issue of whether introduction of Chl f synthase into plants could expand the wavelength range available for oxygenic photosynthesis in crop plants.

AB - Certain cyanobacteria can thrive in environments enriched in far-red light (700–800 nm) due to an acclimation process known as far-red light photoacclimation (FaRLiP). During FaRLiP, about 8% of the Chl a molecules in the photosystems are replaced by Chl f and a very small amount of Chl d. We investigated the spectroscopic properties of Photosystem I (PSI) complexes isolated from wild-type (WT) Synechococcus sp. PCC 7335 and a chlF mutant strain (lacking Chl f synthase) grown in white and far-red light (WL–PSI and FRL–PSI, respectively). WT–FRL–PSI complexes contain Chl f and Chl a but not Chl d. The light-minus dark difference spectrum of the trapping center at high spectral resolution indicates that the special pair in WT–FRL–PSI consists of Chl a molecules with maximum bleaching at 703–704 nm. The action spectrum for photobleaching of the special pair showed that Chl f molecules absorbing at wavelengths up to 800 nm efficiently transfer energy to the trapping center in FRL–PSI complexes to produce a charge-separated state. This is ~ 50 nm further into the near IR than WL–PSI; Chl f has a quantum yield equivalent to that of Chl a in the antenna, i.e., ~ 1.0. PSI complexes from Synechococcus 7002 carrying 3.8 Chl f molecules could promote photobleaching of the special pair by energy transfer at wavelengths longer than WT PSI complexes. Results from these latter studies are directly relevant to the issue of whether introduction of Chl f synthase into plants could expand the wavelength range available for oxygenic photosynthesis in crop plants.

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U2 - 10.1007/s11120-019-00616-x

DO - 10.1007/s11120-019-00616-x

M3 - Article

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AN - SCOPUS:85061004835

VL - 141

SP - 151

EP - 163

JO - Photosynthesis Research

JF - Photosynthesis Research

SN - 0166-8595

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