Structural organization of photosystem I reaction centers

Using a phosphoroscopic attachment to the dichrograph, light-induced circular dichroism spectra have been measured for chlorophyll-protein complexes of Photosystem I. Minor components at 672, 678 and 685 nm are observed in these spectra in addition to the components of dimer splitting of the P700 Q...

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Bibliographic Details
Published in:FEBS letters 1984-07, Vol.173 (1), p.209-212
Main Authors: Karapetyan, N.V., Shubin, V.V., Rakhimberdieva, M.G., Vashchenko, R.G., Bolychevtseva, Yu.V.
Format: Article
Language:English
Subjects:
Biological and medical sciences
C.D
CD, circular dichroism
Cell structures and functions
Chl, chlorophyll
chlorophyll-protein
Chlorophyll-protein complex
Chloroplast, photosynthetic membrane and photosynthesis
Circular dichroism P700
CPI, chlorophyll-protein complex of PSI
Fundamental and applied biological sciences. Psychology
Molecular and cellular biology
P700, primary electron donor of PSI
Photosynthesis
Photosystem I
Pisum sativum
PSI, Photosystem I
reaction centers
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Summary:Using a phosphoroscopic attachment to the dichrograph, light-induced circular dichroism spectra have been measured for chlorophyll-protein complexes of Photosystem I. Minor components at 672, 678 and 685 nm are observed in these spectra in addition to the components of dimer splitting of the P700 Q y transition at 691 and 698 nm. The minor components are due to the Chl672, Chl 678 and Chl 685 forms of antenna chlorophylls, the optical activity of which is changed 2–4% as a result of P700 oxidation. It is suggested that P700 is not an isolated dimer but that it is included in a local complex comprising 8–10 chlorophyll molecules with an exciton level splitting value of 120–140 cm −1.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(84)81048-0