Project/Area Number |
03455014
|
Research Category |
Grant-in-Aid for General Scientific Research (B)
|
Allocation Type | Single-year Grants |
Research Field |
広領域
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Research Institution | KYOTO UNIVERSITY |
Principal Investigator |
KATOH Tetzuya Dept.Botany, Fac.Sci., Kyoto Univ., Ass.Prof., 大学院・理学研究科, 助教授 (30025308)
|
Co-Investigator(Kenkyū-buntansha) |
TANAKA Ayumi Dept.Botany, Fac.Sci., Kyoto Univ., Lecturer, 大学院・理学研究科, 講師 (10197402)
MIMURO Mamoru National Institute for Basic Biology, Assistant, 基礎生物学研究所, 助手 (40142004)
辻 英夫 京都大学, 理学部, 教授 (20025323)
|
Project Period (FY) |
1991 – 1993
|
Project Status |
Completed (Fiscal Year 1993)
|
Budget Amount *help |
¥6,100,000 (Direct Cost: ¥6,100,000)
Fiscal Year 1993: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1992: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1991: ¥4,400,000 (Direct Cost: ¥4,400,000)
|
Keywords | Carotenoid / Fucoxanthin / light-harvesting complexes / Brown algae / Chromophyte / Excitation Energy Transfer / Fucoxanthin Chlorophyll Protein / フコキサンチン / カロテノイド / 光捕捉 / 光合成 / 励起エネルギー / フコキサンチン・クロロフィル複合体 / 光捕捉蛋白 / エネルギー転移 / エネルギ-転移 |
Research Abstract |
Fucoxanthin-Chl a/c protein (FCP), the major light harvesting protein of brown algae and diatoms, is very unstable and its excitation energy transfer between pigments was very readily injured when exposed to detergents conventionally used for isolating various photoactive protens from green plants. We studied on the conditions of FCP isolation from the thalli of brown algae, and revealed that the assemblies of FCP are bound with photochemical reaction center to form complexes which are embedded in thylakoids, like LHCP in green algae. Monomeric form of FCP consisted of a protein with MW 20,226 (in the case of Ectocarpus), 4 Chl a, 1 Chl c and 4 fucoxanthin, and its native form showed an highly efficient energy transfer (higher than 95%) between fucoxanthin*Chl a, Chl c*Chl a. Fucoxanthin bound in FCP showed more red-shifted absorbance than liberated one, showing an absorbance spectrum similar to that dissoved in imidoN-containing, polarsolvets. Exposed to warm temperature (40゚C), the red-shifted FCP turned to green reflecting the blue-shift of fucoxanthin with concomitant loss of CD signals, indicating the disarrangement pigment molecules. However, the resonance Raman spectrum of blue-shifted FCP stayd unaltered from the native FCP,suggesting that fucoxanthin active in excitation energy transfer is highly interacted with Chl a in FCP,and this interaction is responsible to the red shift of fucoxanthin.
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