Conformation of Light-Harvesting Complex II Trimer Depends upon Its Binding Site

Autor: Eunchul Kim, Hisako Kubota-Kawai, Fumihiro Kawai, Makio Yokono, Jun Minagawa

Publikováno v: The Journal of Physical Chemistry B. 126:5855-5865

The light-harvesting complex II (LHCII) trimer in plants functions as a major antenna complex and a quencher to protect it from photooxidative damage. Theoretical studies on the structure of an LHCII trimer have demonstrated that excitation energy tr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7c62fa7430b85bf7c668fd596d02277
https://doi.org/10.1021/acs.jpcb.2c04061

Conformational Changes in Light-Harvesting Complex II Trimer Depending on Its Binding Location

Autor: Eunchul Kim, Hisako Kubota-Kawai, Fumihiro Kawai, Jun Minagawa

In green plants, the light-harvesting complex II (LHCII) trimer functions as a major antenna complex to the photosystem II (PSII) complex and a quencher to protect it from photooxidative damage. Theoretical studies on the structure of the LHCII trime

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4d68c274772d0139822238e033349d0b
https://doi.org/10.21203/rs.3.rs-1258946/v1

Crystal structure of Tam41 cytidine diphosphate diacylglycerol synthase from a Firmicutes bacterium

Autor: Keisuke Kimura, Fumihiro Kawai, Hisako Kubota-Kawai, Yasunori Watanabe, Kentaro Tomii, Rieko Kojima, Kunio Hirata, Yu Yamamori, Toshiya Endo, Yasushi Tamura

Publikováno v: Journal of biochemistry. 171(4)

Translocator assembly and maintenance 41 (Tam41) catalyses the synthesis of cytidine diphosphate diacylglycerol (CDP-DAG), which is a high-energy intermediate phospholipid critical for generating cardiolipin in mitochondria. Although Tam41 is present

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61910554f06da99c7c4326f85fa0a175
https://pubmed.ncbi.nlm.nih.gov/34964897

X-ray structure of an asymmetrical trimeric ferredoxin–photosystem I complex

Autor: Genji Kurisu, Matthias Rögner, Risa Mutoh, Takahisa Ikegami, Pierre Sétif, Hideaki Tanaka, Kanako Shinmura, Hisako Kubota-Kawai, Marc M. Nowaczyk

Publikováno v: Nature Plants
Nature Plants, 2018, 4, pp.218-224. ⟨10.1038/s41477-018-0130-0⟩
Nature Plants, Nature Publishing Group, 2018, 4, pp.218-224. ⟨10.1038/s41477-018-0130-0⟩

International audience; Photosystem I (PSI), a large protein complex located in the thylakoid membrane, mediates the final step in light-driven electron transfer to the stromal electron carrier protein ferredoxin (Fd). Here, we report the first struc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcae45f8087a47c623cf4929940df526
https://doi.org/10.1038/s41477-018-0130-0

X-ray Structure and Nuclear Magnetic Resonance Analysis of the Interaction Sites of the Ga-Substituted Cyanobacterial Ferredoxin

Autor: Matthias Rögner, Young-Ho Lee, Toshiharu Hase, Risa Mutoh, Norifumi Muraki, Genji Kurisu, Takahisa Ikegami, Kanako Shinmura, Hisako Kubota-Kawai, Marc M. Nowaczyk

Publikováno v: Biochemistry. 54(39)

In chloroplasts, ferredoxin (Fd) is reduced by Photosystem I (PSI) and oxidized by Fd-NADP(+) reductase (FNR) that is involved in NADP(+) reduction. To understand the structural basis for the dynamics and efficiency of the electron transfer reaction

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76947cf97e89cad38f237ebe4d7e4634
https://pubmed.ncbi.nlm.nih.gov/26348494