The origin of the long-wavelength fluorescence emission band (77°K) from photosystem I

T. Y. Kuang, J. H. Argyroudi-Akoyunoglou, H. Y. Nakatani, J. Watson, C. J. Arntzen

Research output: Contribution to journalArticle

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Abstract

Isolated photosystem I (PSI)-110 particles, prepared using a minimal concentration of Triton X-100 [J. E. Mullet, J. J. Burke, and C. J. Arntzen (1980) Plant Physiol.65, 814-822] and further subjected to short-term solubilization with sodium dodecyl sulfate (SDS), were resolved into four pigment-containing bands on polyacrylamide gel electrophoresis (PAGE). We have identified these in order of increasing electrophoretic mobility as being (a) CPIa, (b) CPI, (c) the light-harvesting complex of photosystem I (LHC-I), and (d) a free pigment-zone. LHC-I had an absorption maximum in the red at 668-669 nm and a shoulder at 650 nm, which was resolved by its first-derivative spectrum to indicate the presence of chlorophyll b. LHC-I exhibited a 77 °K fluorescence emission maximum at 729-730 nm. The 77°K fluorescence emission maxima of CPIa and CPI, excised from the gel, were at 729 and 722 nm, respectively. The LHC-I band, excised from the gel and rerun on dissociating SDS-PAGE, was resolved into two polypeptide doublets of 24-22.5 and 21-20.5 kDa. The CPIa band under similar conditions was resolved into polypeptides of 68, 24, 22.5, 21, 20.5, 19, 15, and 14 kDa; on the contrary, CPI contained only the 68-kDa polypeptide. When intact thylakoids were subjected to "nondenaturing" SDS-PAGE, LHC-I comigrated with an oligomeric form (dimer) of the light-harvesting chlorophyll a/b pigment-protein that preferentially serves photosystem II (LHCP-II). When this combined LHC-I/ LHCP-II pigment-protein band was prepared by SDS-PAGE from isolated stroma lamellae, it exhibited a long-wavelength fluorescence band near 730 nm at 77 °K. When a similar preparation was obtained from sucrose density gradients containing SDS [J. Argyroudi-Akoyunoglou and H. Thomou (1981) FEBS Lett.135, 171-181], it was found to be enriched in a 21-kDa polypeptide. The data suggest that the 21-kDa polypeptide of LHC-I is the chlorophyll-containing polypeptide responsible for the long-wavelength fluorescence of LHC-I; other polypeptides in the complex (20.5, 22.5, and 24 kDa) presumably bind chlorophyll and also serve an antennae function.

Original languageEnglish (US)
Pages (from-to)618-627
Number of pages10
JournalArchives of Biochemistry and Biophysics
Volume235
Issue number2
DOIs
StatePublished - 1984
Externally publishedYes

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Photosystem I Protein Complex
Fluorescence
Wavelength
Light
Sodium Dodecyl Sulfate
Peptides
Electrophoresis
Pigments
Polyacrylamide Gel Electrophoresis
Chlorophyll
Gels
Electrophoretic mobility
Thylakoids
Photosystem II Protein Complex
Octoxynol
Dimers
Sucrose
Proteins
Antennas
Derivatives

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Kuang, T. Y., Argyroudi-Akoyunoglou, J. H., Nakatani, H. Y., Watson, J., & Arntzen, C. J. (1984). The origin of the long-wavelength fluorescence emission band (77°K) from photosystem I. Archives of Biochemistry and Biophysics, 235(2), 618-627. https://doi.org/10.1016/0003-9861(84)90236-4

The origin of the long-wavelength fluorescence emission band (77°K) from photosystem I. / Kuang, T. Y.; Argyroudi-Akoyunoglou, J. H.; Nakatani, H. Y.; Watson, J.; Arntzen, C. J.

In: Archives of Biochemistry and Biophysics, Vol. 235, No. 2, 1984, p. 618-627.

Research output: Contribution to journalArticle

Kuang, TY, Argyroudi-Akoyunoglou, JH, Nakatani, HY, Watson, J & Arntzen, CJ 1984, 'The origin of the long-wavelength fluorescence emission band (77°K) from photosystem I', Archives of Biochemistry and Biophysics, vol. 235, no. 2, pp. 618-627. https://doi.org/10.1016/0003-9861(84)90236-4
Kuang, T. Y. ; Argyroudi-Akoyunoglou, J. H. ; Nakatani, H. Y. ; Watson, J. ; Arntzen, C. J. / The origin of the long-wavelength fluorescence emission band (77°K) from photosystem I. In: Archives of Biochemistry and Biophysics. 1984 ; Vol. 235, No. 2. pp. 618-627.
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AU - Watson, J.

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