دورية أكاديمية
Structure of a retinal chromophore of dark-adapted middle rhodopsin as studied by solid-state nuclear magnetic resonance spectroscopy
| العنوان: | Structure of a retinal chromophore of dark-adapted middle rhodopsin as studied by solid-state nuclear magnetic resonance spectroscopy |
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| المؤلفون: | Izuru Kawamura, Hayato Seki, Seiya Tajima, Yoshiteru Makino, Arisu Shigeta, Takashi Okitsu, Akimori Wada, Akira Naito, Yuki Sudo |
| المصدر: | Biophysics and Physicobiology, Vol 18 (2021) |
| بيانات النشر: | The Biophysical Society of Japan, 2021. |
| سنة النشر: | 2021 |
| المجموعة: | LCC:Biology (General) LCC:Physiology LCC:Physics |
| مصطلحات موضوعية: | microbial rhodopsin, retinal isomers, nuclear magnetic resonance, protonated schiff base, chemical shifts, Biology (General), QH301-705.5, Physiology, QP1-981, Physics, QC1-999 |
| الوصف: | Middle rhodopsin (MR) found from the archaeon Haloquadratum walsbyi is evolutionarily located between two different types of rhodopsins, bacteriorhodopsin (BR) and sensory rhodopsin II (SRII). Some isomers of the chromophore retinal and the photochemical reaction of MR are markedly different from those of BR and SRII. In this study, to obtain the structural information regarding its active center (i.e., retinal), we subjected MR embedded in lipid bilayers to solid-state magic-angle spinning nuclear magnetic resonance (NMR) spectroscopy. The analysis of the isotropic 13C chemical shifts of the retinal chromophore revealed the presence of three types of retinal configurations of dark-adapted MR: (13-trans, 15-anti (all-trans)), (13-cis, 15-syn), and 11-cis isomers. The higher field resonance of the 20-C methyl carbon in the all-trans retinal suggested that Trp182 in MR has an orientation that is different from that in other microbial rhodopsins, owing to the changes in steric hindrance associated with the 20-C methyl group in retinal. 13Cζ signals of Tyr185 in MR for all-trans and 13-cis, 15-syn isomers were discretely observed, representing the difference in the hydrogen bond strength of Tyr185. Further, 15N NMR analysis of the protonated Schiff base corresponding to the all-trans and 13-cis, 15-syn isomers in MR showed a strong electrostatic interaction with the counter ion. Therefore, the resulting structural information exhibited the property of stable retinal conformations of dark-adapted MR. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2189-4779 |
| العلاقة: | https://doaj.org/toc/2189-4779Test |
| DOI: | 10.2142/biophysico.bppb-v18.019 |
| الوصول الحر: | https://doaj.org/article/e75ffead0e1d40a0a2eb98913c1c4f62Test |
| رقم الانضمام: | edsdoj.75ffead0e1d40a0a2eb98913c1c4f62 |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 21894779 |
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| DOI: | 10.2142/biophysico.bppb-v18.019 |