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The site of regulation of light capture in Symbiodinium: Does the peridinin–chlorophyll a–protein detach to regulate light capture?

Journal Article · · Biochimica et Biophysica Acta - Bioenergetics
 [1];  [2];  [3];  [3];  [4]
  1. Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory; MSU DOE Plant Research Laboratory
  2. Michigan State Univ., East Lansing, MI (United States)
  3. Univ. of Technology, Sydney, NSW (Australia)
  4. Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
+ Show Author Affiliations
Dinoflagellates from the genus Symbiodinium form symbiotic associations with cnidarians including corals and anemones. The photosynthetic apparatuses of these dinoflagellates possess a unique photosynthetic antenna system incorporating the peridinin–chlorophyll a–protein (PCP). It has been proposed that the appearance of a PCP-specific 77 K fluorescence emission band around 672–675 nm indicates that high light treatment results in PCP dissociation from intrinsic membrane antenna complexes, blocking excitation transfer to the intrinsic membrane-bound antenna complexes, chlorophyll a–chlorophyll c2–peridinin–protein-complex (acpPC) and associated photosystems (Reynolds et al., 2008 Proc Natl Acad Sci USA 105:13674–13678).We have tested this model using time-resolved fluorescence decay kinetics in conjunction with global fitting to compare the time-evolution of the PCP spectral bands before and after high light exposure. Here, our results show that no long-lived PCP fluorescence emission components appear either before or after high light treatment, indicating that the efficiency of excitation transfer from PCP to membrane antenna systems remains efficient and rapid even after exposure to high light. The apparent increased relative emission at around 675 nm was, instead, caused by strong preferential exciton quenching of the membrane antenna complexes associated with acpPC and reaction centers. This strong non-photochemical quenching (NPQ) is consistent with the activation of xanthophyll-associated quenching mechanisms and the generally-observed avoidance in nature of long-lived photoexcited states that can lead to oxidative damage. The acpPC component appears to be the most strongly quenched under high light exposure suggesting that it houses the photoprotective exciton quencher.
Research Organization:
Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
Sponsoring Organization:
Australian Research Council (ARC); USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22). Chemical Sciences, Geosciences & Biosciences Division
Grant/Contract Number:
FG02-91ER20021
OSTI ID:
1608553
Journal Information:
Biochimica et Biophysica Acta - Bioenergetics, Journal Name: Biochimica et Biophysica Acta - Bioenergetics Journal Issue: 8 Vol. 1837; ISSN 0005-2728
Publisher:
ElsevierCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (3)

Light-induced formation of dimeric LHCII journal April 2017
Charting the native architecture of thylakoid membranes with single-molecule precision journal January 2019
Novel Adaptive Photosynthetic Characteristics of Mesophotic Symbiotic Microalgae within the Reef-Building Coral, Stylophora pistillata journal October 2016

Figures / Tables (7)

Figure 1(p. 8)figure Figure 1
Table 1(p. 9)table Table 1
Figure 2(p. 10)figure Figure 2
Table 2(p. 11)table Table 2
Figure 3(p. 12)figure Figure 3
Figure 4(p. 13)figure Figure 4
Figure 5(p. 14)figure Figure 5

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Non-photochemical quenching
Peridinin–chlorophyll a–protein
Photoprotection
Photosynthesis