Molecular organisation of the chlorophyll a/c light-harvesting complex of Pleurochloris meiringensis (Xanthophyceae). Pigment binding and secondary structure of the protein

C. Büchel, G. Garab

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 languageEnglish
Pages (from-to)191-194
Number of pages4
JournalJournal of Photochemistry and Photobiology, B: Biology
Volume42
Issue number3
DOIs
Publication statusPublished - Mar 1998

Fingerprint

Xanthophyceae
circular dichroism spectroscopy
protein secondary structure
Secondary Protein Structure
light harvesting complex
chlorophylls
Chlorophyll
Circular Dichroism
pigments
Pigments
dichroism
Dichroism
proteins
Proteins
chlorophyll
Light
wavelengths
Light-Harvesting Protein Complexes
Circular dichroism spectroscopy
digitonin

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

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title = "Molecular organisation of the chlorophyll a/c light-harvesting complex of Pleurochloris meiringensis (Xanthophyceae). Pigment binding and secondary structure of the protein",
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.",
keywords = "Algae, Circular dichroism, Light-harvesting complex, Photosynthesis, Secondary structure of proteins",
author = "C. B{\"u}chel and G. Garab",
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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.

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