Biochemical and Spectroscopic Characterizations of a Hybrid Light-Harvesting Reaction Center Core Complex
Autor: | Zheng-Yu Wang-Otomo, Mizuki Takenouchi, Michie Imanishi, Kengo Suzuki, Shinji Takenaka, Seiji Akimoto, Kanako Hashimoto, Yukihiro Kimura, Rikako Kishi, Michael T. Madigan, Kenji V. P. Nagashima |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Photosynthetic reaction centre Light-Harvesting Protein Complexes Rhodobacter sphaeroides Protein aggregation 010402 general chemistry 01 natural sciences Biochemistry Chromatiaceae Metal 03 medical and health sciences Protein Aggregates Bacterial Proteins Thermal stability Binding site Binding Sites biology Strain (chemistry) Chemistry Protein Stability biology.organism_classification 0104 chemical sciences Crystallography 030104 developmental biology Energy Transfer visual_art visual_art.visual_art_medium Calcium Heterologous expression Protein Binding |
Zdroj: | Biochemistry. 57(30) |
ISSN: | 1520-4995 |
Popis: | The light-harvesting 1 reaction center (LH1-RC) complex from Thermochromatium tepidum exhibits a largely red-shifted LH1 Qy absorption at 915 nm due to binding of Ca2+, resulting in an “uphill” energy transfer from LH1 to the reaction center (RC). In a recent study, we developed a heterologous expression system (strain TS2) to construct a functional hybrid LH1-RC with LH1 from Tch. tepidum and the RC from Rhodobacter sphaeroides [Nagashima, K. V. P., et al. (2017) Proc. Natl. Acad. Sci. U. S. A. 114, 10906]. Here, we present detailed characterizations of the hybrid LH1-RC from strain TS2. Effects of metal cations on the phototrophic growth of strain TS2 revealed that Ca2+ is an indispensable element for its growth, which is also true for Tch. tepidum but not for Rba. sphaeroides. The thermal stability of the TS2 LH1-RC was strongly dependent on Ca2+ in a manner similar to that of the native Tch. tepidum, but interactions between the heterologous LH1 and RC became relatively weaker in strain TS2. A Fourier... |
Databáze: | OpenAIRE |
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