Time-resolved fluorescence studies on the internal motionof chlorophyll a of light-harvesting chlorophylla/b-protein complex in lipid membranes

Makio Furuichi, Etsuko Nishimoto, Toshiaki Koga, Shoji Yamashita

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

By analyzing the steady state and time-resolved fluorescence anisotropy, the internal motions of chlorophyll a of light-harvesting chlorophyll a/b-protein complex (LHCII) were characterized in a dimyristoylphosphatidylcholine (DMPC) liposome. Corresponding to the thermotropic phase of the membrane, chlorophyll a showed an unique internal motion in LHCII. At the gel phase, two motional components, one fast and the other slow, were observed, which would originate in the heterogeneity of the mutual orientation and the binding site of the chlorophyll a in LHCII. Interestingly, the faster motion was suppressed and only the slower segmental rotation with the larger motional amplitude was allowed on the phasetransition to a liquid crystalline phase.

Original languageEnglish
Pages (from-to)1623-1627
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Volume64
Issue number8
DOIs
Publication statusPublished - Jan 1 2000

Fingerprint

Membrane Lipids
Fluorescence
Light
Chlorophyll Binding Proteins
Dimyristoylphosphatidylcholine
Proteins
Fluorescence Polarization
Liposomes
Gels
Binding Sites
Anisotropy
Membranes
Crystalline materials
chlorophyll a
Liquids

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

Cite this

Time-resolved fluorescence studies on the internal motionof chlorophyll a of light-harvesting chlorophylla/b-protein complex in lipid membranes. / Furuichi, Makio; Nishimoto, Etsuko; Koga, Toshiaki; Yamashita, Shoji.

In: Bioscience, Biotechnology and Biochemistry, Vol. 64, No. 8, 01.01.2000, p. 1623-1627.

Research output: Contribution to journalArticle

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