<博士論文>
好熱性藍藻の光化学系I膜複合体の安定化剤の検索とその特徴

作成者
論文調査委員
本文言語
学位授与年度
学位授与大学
学位
学位種別
出版タイプ
アクセス権
JaLC DOI
概要 For sustainable society, it is required to supply more clean energy including photovoltaics, bio-fuels, bio-diesel, hydrogen gas and so on. The photosynthesis is the conversion of light energy into ch...emical energy. This reaction is carried out by the absorption of solar photons in two serial photosynthetic electrontransport reaction centers called as photosystem I and II (PS-I and PS-II, respectively) (1, 2). The PS-II complex photooxidizes water to molecular oxygen, and the PS-I complex photoreduces NADP+ to NADPH. PS-I is a thylakoid transmembrane protein complex. In order to utilize the intense photocatalytic properties of PS-I for the energy production, vigorous active researches have been carried out (3-8). The crystal structure of PS-I from the thermophilic cyanobacterium Thermosynechoccus elongatus was solved by Jordan et al (9). The trimeric protein complex has a molecular mass of 1.07 MDa and consists of 36 proteins to which 381 co-factors are non-covalently attached. Each monomer of the polymeric complex consists of 12 proteins and 9 of these proteins per monomer feature a network of 34 transmembrane α-helices (for a total of 102 helices in the trimer) that are buried within the lipid bilayer. The large number of transmembrane helices and extensive interactions with the thylakoid membranes have been problematic in developing protocols for the efficient purification, solubilization and crystallization of the native PS-I super-complex, complete with its associated antenna pigments and co-factors. For efficient production of energy, photosynthetic complexes might offer attractive architecture for future generation of circuitry where molecular components are organized by a macromolecular scaffold. However, like other complex structure of proteins, PS-I is also soft materials, which is optimized for operation in a lipid bilayer interface between aqueous solutions. For preservation of protein conformation and maintenance or even increase of its activity in solution during reaction, stabilization of multi-protein complex is pivotal. Thus, in this thesis I studied the stabilization and activation of multi-protein complex by various oligo-peptides and poly-amino acids, and their mechanism on stabilization and activity enhancement.続きを見る
目次 Abbreviations
General introduction
Chapter 1. Peptide surfactants for stabilization of functional photosystem I membrane complex in aqueous solution
Chapter 2. Enhancement of the electron transfer activity on photosystem I by cationic polypeptide surfactants in aqueous solution
General conclusions
Publications
Acknowledgements
References

本文ファイル

pdf agr654 pdf 850 KB 333 本文
pdf agr654_abstract pdf 167 KB 273 要旨

詳細

レコードID
査読有無
キーワード
報告番号
学位記番号
授与日(学位/助成/特許)
受理日
部局
所蔵場所
所蔵場所
注記
登録日 2013.07.10
更新日 2023.11.21

この資料を見た人はこんな資料も見ています