4.5 Article

Multiple LHCII antennae can transfer energy efficiently to a single Photosystem I

期刊

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1858, 期 5, 页码 371-378

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2017.02.012

关键词

Excitation energy transfer; State transitions; Light-harvesting complex; Time-resolved fluorescence

资金

  1. Marie Sklodowska Curie IF grant [655542]
  2. Netherlands Organisation for Scientific Research (NWO) [016.161.038, 865.10.013]
  3. European Research Council (ERC) [281341]
  4. Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-FG02-98ER20310]
  5. Marie Curie Actions (MSCA) [655542] Funding Source: Marie Curie Actions (MSCA)

向作者/读者索取更多资源

Photosystems I and II (PSI and PSII) work in series to drive oxygenic photosynthesis. The two photosystems have different absorption spectra, therefore changes in light quality can lead to imbalanced excitation of the photosystems and a loss in photosynthetic efficiency. In a short-term adaptation response termed state transitions, excitation energy is directed to the light-limited photosystem. In higher plants a special pool of LHCII antennae, which can be associated with either PSI or PSII, participates in these state transitions. It is known that one LHCII antenna can associate with the PsaH site of PSI. However, membrane fractions were recently isolated in which multiple LHCII antennae appear to transfer energy to PSI. We have used time-resolved fluorescence-streak camera measurements to investigate the energy transfer rates and efficiency in these membrane fractions. Our data show that energy transfer from LHCII to PSI is relatively slow. Nevertheless, the trapping efficiency in supercomplexes of PSI with similar to 2.4 LHCIIs attached is 94%.The absorption cross section of PSI can thus be increased with similar to 65% without having significant loss in quantum efficiency. Comparison of the fluorescence dynamics of PSI-LHCII complexes, isolated in a detergent or located in their native membrane environment, indicates that the environment influences the excitation energy transfer rates in these complexes. This demonstrates the importance of studying membrane protein complexes in their natural environment. (C) 2017 Elsevier B.V. All rights reserved.

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