@inproceedings{oai:repo.qst.go.jp:00082906,
 author = {Shigeki, Arai and Rumi, Shimizu and Motoyasu, Adachi and Mitsuhiro, Hirai and Shigeki, Arai and Rumi, Shimizu and Motoyasu, Adachi},
 book = {Photon Factory Activity Report},
 issue = {38},
 month = {Jun},
 note = {The iron-sulfur cluster assembly 1 homolog clISCA1 of Columba livia (pigeon) interacts with a quantum biosensor protein clCRY4.  The clCRY4/clISCA1 complex tends to orientate along the weak external magnetic-field lines (0.4–10G) under blue light, suggesting that clISCA1 might assist the function of clCRY4.  It was expected that the Fe-S cluster binging to clISCA1 might improve the magnetic property of clISCA1.  In order to elucidate the Fe-S cluster binging mechanism of clISCA1, we conducted the small angle X-ray scattering analysis coupled with size exclusion chromatography analysis (SEC-SAXS) and UV/Vis spectroscopy.  The result suggests that the globular protomers of clISCA1 form columnar oligomers, and Fe-S cluster binding sites are formed between clISCA1 protomers in a columnar oligomer. Periodic and regular binding of Fe-S clusters along the long axis of the columnar oligomer may improve the magnetic susceptibility and the magnetic anisotropy of the clISCA1 oligomer and the clCRY4/clISCA1 complex.},
 publisher = {高エネルギー加速器研究機構},
 title = {Fe-S cluster binding mechanism of pigeon's ISCA1 clarified by SEC-SAXS},
 volume = {2021},
 year = {2021}
}