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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Rogl H,Kühlbrandt W,Barth Adoi
10.1021/bi034114+subject
Has Abstractpub_date
2003-09-02 00:00:00pages
10223-8issue
34eissn
0006-2960issn
1520-4995journal_volume
42pub_type
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