Abstract
In our previous study by means of circular dichroism (CD) spectroscopy we have shown that the pigment organisation in the chlorophyll a/c light harvesting complex (Chl a/c LHC) isolated from Pleurochloris meiringensis significantly differs from the architecture of the main Chl a/c light harvesting antenna complexes of higher plants. In this work we meusured the CD spectra in the far-UV.between 190 nm and 240 nm. and investigated the variations of the secondary structure of the protein upon treatments which affect the binding of the long wavelength Chl a. We found that low concentrations ( ≤ 5%) of acetone, which had no noticeable effect on the ( -)679 nm CD band, drastically reduced the α-helical content of the protein. In contrast, amounts of digitonin, which completely abolished this intense.non-conservative CD band of Chl a. induced only minor changes in the secondary structure of the protein complex. These data suggest that the binding site of the long-wavelength absorbing Chl a is found in a position deeply buried in the protein, and it is most likely co-ordinated by two helices.
| Original language | English |
|---|---|
| Pages (from-to) | 191-194 |
| Number of pages | 4 |
| Journal | Journal of Photochemistry and Photobiology, B: Biology |
| Volume | 42 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Mar 1998 |
Fingerprint
Keywords
- Algae
- Circular dichroism
- Light-harvesting complex
- Photosynthesis
- Secondary structure of proteins
ASJC Scopus subject areas
- Plant Science
- Bioengineering
- Physical and Theoretical Chemistry
Cite this
Molecular organisation of the chlorophyll a/c light-harvesting complex of Pleurochloris meiringensis (Xanthophyceae). Pigment binding and secondary structure of the protein. / Büchel, C.; Garab, G.
In: Journal of Photochemistry and Photobiology, B: Biology, Vol. 42, No. 3, 03.1998, p. 191-194.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular organisation of the chlorophyll a/c light-harvesting complex of Pleurochloris meiringensis (Xanthophyceae). Pigment binding and secondary structure of the protein
AU - Büchel, C.
AU - Garab, G.
PY - 1998/3
Y1 - 1998/3
N2 - In our previous study by means of circular dichroism (CD) spectroscopy we have shown that the pigment organisation in the chlorophyll a/c light harvesting complex (Chl a/c LHC) isolated from Pleurochloris meiringensis significantly differs from the architecture of the main Chl a/c light harvesting antenna complexes of higher plants. In this work we meusured the CD spectra in the far-UV.between 190 nm and 240 nm. and investigated the variations of the secondary structure of the protein upon treatments which affect the binding of the long wavelength Chl a. We found that low concentrations ( ≤ 5%) of acetone, which had no noticeable effect on the ( -)679 nm CD band, drastically reduced the α-helical content of the protein. In contrast, amounts of digitonin, which completely abolished this intense.non-conservative CD band of Chl a. induced only minor changes in the secondary structure of the protein complex. These data suggest that the binding site of the long-wavelength absorbing Chl a is found in a position deeply buried in the protein, and it is most likely co-ordinated by two helices.
AB - In our previous study by means of circular dichroism (CD) spectroscopy we have shown that the pigment organisation in the chlorophyll a/c light harvesting complex (Chl a/c LHC) isolated from Pleurochloris meiringensis significantly differs from the architecture of the main Chl a/c light harvesting antenna complexes of higher plants. In this work we meusured the CD spectra in the far-UV.between 190 nm and 240 nm. and investigated the variations of the secondary structure of the protein upon treatments which affect the binding of the long wavelength Chl a. We found that low concentrations ( ≤ 5%) of acetone, which had no noticeable effect on the ( -)679 nm CD band, drastically reduced the α-helical content of the protein. In contrast, amounts of digitonin, which completely abolished this intense.non-conservative CD band of Chl a. induced only minor changes in the secondary structure of the protein complex. These data suggest that the binding site of the long-wavelength absorbing Chl a is found in a position deeply buried in the protein, and it is most likely co-ordinated by two helices.
KW - Algae
KW - Circular dichroism
KW - Light-harvesting complex
KW - Photosynthesis
KW - Secondary structure of proteins
UR - http://www.scopus.com/inward/record.url?scp=0032032790&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032032790&partnerID=8YFLogxK
U2 - 10.1016/S1011-1344(98)00069-4
DO - 10.1016/S1011-1344(98)00069-4
M3 - Article
VL - 42
SP - 191
EP - 194
JO - Journal of Photochemistry and Photobiology B: Biology
JF - Journal of Photochemistry and Photobiology B: Biology
SN - 1011-1344
IS - 3
ER -