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Journal Article

Light-induced changes in the chemical bond structure of light harvesting complex II probed by FTIR spectroscopy.

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Rogl,  Hans
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Rogl, H., Kühlbrandt, W., & Barth, A. (2003). Light-induced changes in the chemical bond structure of light harvesting complex II probed by FTIR spectroscopy. Biochemistry, 42(34): doi: 10.1021/bi034114+, pp. 10223-10228. doi:10.1021/bi034114+.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DB49-0
Abstract
Light-harvesting complex II (LHC-II) regulates the light energy distribution between photosystem I and II in plants. This process is mediated by phosphorylation of the LHC-II protein, which depends on the oxidation state of photosynthetic electron carriers. In addition to this regulatory mechanism, it has recently been proposed that light can directly induce a conformational change in isolated LHC-II. To provide biophysical evidence for such a conformational change in the protein, we studied infrared absorbance changes in isolated LHC-II upon exposure to light flashes. Compared to the signals obtained with other proteins that exhibit well-characterized conformational changes, the signal in the LHC-II difference spectra is very weak. The position of the difference bands coincides with the main IR absorption bands of chlorophyll. We conclude that there are no detectable light-induced changes in the LHC protein structure and attribute the observed IR signals to light-induced chlorophyll degradation.