TY - JOUR
T1 - Investigation of the molecular mechanism of the blue-light-specific excitation energy quenching in the plant antenna complex LHCII
AU - Gruszecki, Wieslaw I.
AU - Zubik, Monika
AU - Luchowski, Rafal
AU - Grudzinski, Wojciech
AU - Gospodarek, Malgorzata
AU - Szurkowski, Janusz
AU - Gryczynski, Zygmunt
AU - Gryczynski, Ignacy
N1 - Funding Information:
This research was financed by the Ministry of Science and Higher Education of Poland from the funds for science in the years 2008–2011 within the research project N N303 285034.
PY - 2011/3/15
Y1 - 2011/3/15
N2 - Excitation of the major photosynthetic antenna complex of plants, LHCII, with blue light (470. nm) provides an advantage to plants, as it gives rise to chlorophyll a fluorescence lifetimes shorter than with excitation with red light (635. nm). This difference is particularly pronounced in fluorescence emission wavelengths longer than 715. nm. Illumination of LHCII preparation with blue light additionally induces fluorescence quenching, which develops on a minute timescale. This effect is much less efficient when induced by red light, despite the equalized energy absorbed in both the spectral regions. Simultaneous analysis of the fluorescence and photoacoustic signals in LHCII demonstrated that the light-driven fluorescence quenching is not associated with an increase in heat emission. Instead, a reversible light-induced conformational transformation of the protein takes place, as demonstrated by the FTIR technique. These findings are discussed in terms of the blue-light-specific excitation energy quenching in LHCII, which may have photoprotective applications.
AB - Excitation of the major photosynthetic antenna complex of plants, LHCII, with blue light (470. nm) provides an advantage to plants, as it gives rise to chlorophyll a fluorescence lifetimes shorter than with excitation with red light (635. nm). This difference is particularly pronounced in fluorescence emission wavelengths longer than 715. nm. Illumination of LHCII preparation with blue light additionally induces fluorescence quenching, which develops on a minute timescale. This effect is much less efficient when induced by red light, despite the equalized energy absorbed in both the spectral regions. Simultaneous analysis of the fluorescence and photoacoustic signals in LHCII demonstrated that the light-driven fluorescence quenching is not associated with an increase in heat emission. Instead, a reversible light-induced conformational transformation of the protein takes place, as demonstrated by the FTIR technique. These findings are discussed in terms of the blue-light-specific excitation energy quenching in LHCII, which may have photoprotective applications.
KW - Blue light effect
KW - FLIM
KW - LHCII
KW - Photoprotection
KW - Xanthophylls
UR - http://www.scopus.com/inward/record.url?scp=79251598507&partnerID=8YFLogxK
U2 - 10.1016/j.jplph.2010.08.009
DO - 10.1016/j.jplph.2010.08.009
M3 - Article
C2 - 20950892
AN - SCOPUS:79251598507
SN - 0176-1617
VL - 168
SP - 409
EP - 414
JO - Journal of Plant Physiology
JF - Journal of Plant Physiology
IS - 5
ER -