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Biochim Biophys Acta Bioenerg. 2017 May;1858(5):371-378. doi: 10.1016/j.bbabio.2017.02.012. Epub 2017 Feb 22.

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

Author information

1
Laboratory of Biophysics, Wageningen University, P.O. Box 8128, 6700 ET Wageningen, The Netherlands.
2
Department of Biological Sciences, Biochemistry and Molecular Biology Section, Louisiana State University, Baton Rouge, LA 70803, United States.
3
Department of Physics and Astronomy and Institute for Lasers, Life and Biophotonics, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands.
4
Laboratory of Biophysics, Wageningen University, P.O. Box 8128, 6700 ET Wageningen, The Netherlands; MicroSpectroscopy Centre, Wageningen University, P.O. Box 8128, 6700 ET Wageningen, The Netherlands.
5
Laboratory of Biophysics, Wageningen University, P.O. Box 8128, 6700 ET Wageningen, The Netherlands. Electronic address: emilie.wientjes@wur.nl.

Abstract

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 ~2.4 LHCIIs attached is 94%. The absorption cross section of PSI can thus be increased with ~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.

KEYWORDS:

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

PMID:
28237494
DOI:
10.1016/j.bbabio.2017.02.012
[Indexed for MEDLINE]
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