Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base
Heliorhodopsin (HeR) is a novel class of retinal proteins discovered in 2018 [1]. HeR contains an all-trans-retinal as a chromophore, which is covalently bound to a lysine residue through a protonated Schiff base linkage. Although amino acid sequences of HeR are largely different from those of type-...
| Main Authors: | , , , , |
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| Other Authors: | |
| Format: | Conference Paper |
| Language: | English |
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2020
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| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/144338 |
| _version_ | 1826127640600248320 |
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| author | Urui, Taito Otomo, Akihiro Mizuno, Misao Kandori, Hideki Mizutani, Yasuhisa |
| author2 | Asian Spectroscopy Conference 2020 |
| author_facet | Asian Spectroscopy Conference 2020 Urui, Taito Otomo, Akihiro Mizuno, Misao Kandori, Hideki Mizutani, Yasuhisa |
| author_sort | Urui, Taito |
| collection | NTU |
| description | Heliorhodopsin (HeR) is a novel class of retinal proteins discovered in 2018 [1]. HeR contains an all-trans-retinal as a chromophore, which is covalently bound to a lysine residue through a protonated Schiff base linkage. Although amino acid sequences of HeR are largely different from those of type-1 rhodopsins, a family of HeR shares the seven-transmembrane helix motif. Photoexcitation of the all-trans-retinal chromophore results in isomerization to a 13-cis form. This isomerization initiates a photocycle involving a series of intermediates, which are similar to those observed for type-1 rhodopsins. HeR has a long-lived intermediate in its photocycle, which is named the O intermediate, suggesting that the function of HeR is light sensing. In order to understand the functional role of the O intermediate, we investigated the chromophore structure in two HeRs, HeR 48C12 and T. archaeon HeR, using time-resolved resonance Raman spectroscopy. |
| first_indexed | 2024-10-01T07:11:50Z |
| format | Conference Paper |
| id | ntu-10356/144338 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:11:50Z |
| publishDate | 2020 |
| record_format | dspace |
| spelling | ntu-10356/1443382020-10-29T20:12:15Z Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base Urui, Taito Otomo, Akihiro Mizuno, Misao Kandori, Hideki Mizutani, Yasuhisa Asian Spectroscopy Conference 2020 Institute of Advanced Studies Science::Chemistry Rhodopsin Retinal Chromophore Heliorhodopsin (HeR) is a novel class of retinal proteins discovered in 2018 [1]. HeR contains an all-trans-retinal as a chromophore, which is covalently bound to a lysine residue through a protonated Schiff base linkage. Although amino acid sequences of HeR are largely different from those of type-1 rhodopsins, a family of HeR shares the seven-transmembrane helix motif. Photoexcitation of the all-trans-retinal chromophore results in isomerization to a 13-cis form. This isomerization initiates a photocycle involving a series of intermediates, which are similar to those observed for type-1 rhodopsins. HeR has a long-lived intermediate in its photocycle, which is named the O intermediate, suggesting that the function of HeR is light sensing. In order to understand the functional role of the O intermediate, we investigated the chromophore structure in two HeRs, HeR 48C12 and T. archaeon HeR, using time-resolved resonance Raman spectroscopy. Published version 2020-10-29T04:27:56Z 2020-10-29T04:27:56Z 2020 Conference Paper Urui, T., Otomo, A., Mizuno, M., Kandori, H., & Mizutani, Y. (2020). Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base. Proc. Of the 7th Asian Spectroscopy Conference (ASC 2020). doi:10.32655/ASC_8-10_Dec2020.62 https://hdl.handle.net/10356/144338 10.32655/ASC_8-10_Dec2020.62 en © 2020 Nanyang Technological University. application/pdf |
| spellingShingle | Science::Chemistry Rhodopsin Retinal Chromophore Urui, Taito Otomo, Akihiro Mizuno, Misao Kandori, Hideki Mizutani, Yasuhisa Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base |
| title | Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base |
| title_full | Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base |
| title_fullStr | Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base |
| title_full_unstemmed | Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base |
| title_short | Chromophore structure in a long-lived intermediate of heliorhodopsins : switching of a hydrogen bonding partner of protonated Schiff base |
| title_sort | chromophore structure in a long lived intermediate of heliorhodopsins switching of a hydrogen bonding partner of protonated schiff base |
| topic | Science::Chemistry Rhodopsin Retinal Chromophore |
| url | https://hdl.handle.net/10356/144338 |
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