Molecular Assemblies of Chlorophyll Derivatives by Light-Harvesting Polypeptides and Their Model Polypeptides.

Accession number;99A0228225
Title;Molecular Assemblies of Chlorophyll Derivatives by Light-Harvesting Polypeptides and Their Model Polypeptides.
Author; KASHIWADA AYUMI (Nagoya Inst. of Technol.) YAMADA SHUHEI (Nagoya Inst. of Technol.) WATANABE HIROYUKI (Nagoya Inst. of Technol.) YAMASHITA KEIJI (Nagoya Inst. of Technol.) NANGO MAMORU (Nagoya Inst. of Technol.) TSUDA KAZUICHI (Nagoya Inst. of Technol.) TANAKA TOSHIKI (Seibutsubunshikogakuken)
Journal Title;Abstracts. Symposium on Biofunctional Chemistry
Journal Code:L0836A
ISSN:
VOL.13th;NO.;PAGE.109-111(1998)
Figure&Table&Reference;
Pub. Country;Japan
Language;Japanese
Abstract;Molecular assembly of BChla by model polypeptide having the same sequence as the core region of the LH-.BETA. polypeptide from Rb. sphaeroides (type 1) and analogoues in each of which one highly conserved amino acid. Trp+9 or Trp+6 were changed to Phe (type 3 and 4) in octylglycopyranoside(OG) micelle was examined. UV-vis. spectra of BChla with type 1 showed that the Qy band was shifted from 821nm to 847nm, indicating that type 1 can form subunit-type complexes with BChla (Qy band of BChla: 821nm) and further complexes are formed (Qy band of BChla: 847nm) under cooling condition (4.DEG.C.). On the other hand, UV-vis. spectra of BChla with type 3 or 4 showed 815nm absorbance at 0.78% OG solution but further red-shift was not observed at 4.DEG.C.. These results indicated that Trp residues on C terminus of LH-.BETA. polypeptide play an important role on the organization of BChla. (author abst.)