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P., Lodowski, D. T., Elstner, M., Hegemann, P., Brown, L. S., Kandori, H. Microbial and animal rhodopsins: Structures, functions, and molecular mechanisms. Chem. Rev. 114, 126\u2013163 (2014). https:\/\/doi.org\/10.1021\/cr4003769","DOI":"10.1021\/cr4003769"},{"key":"2","doi-asserted-by":"crossref","unstructured":"[2] Terakita, A. The opsins. Genome Biol. 6, 213 (2005). https:\/\/doi.org\/10.1186\/gb-2005-6-3-213","DOI":"10.1186\/gb-2005-6-3-213"},{"key":"3","doi-asserted-by":"crossref","unstructured":"[3] Palczewski, K. Chemistry and biology of vision. J. Biol. Chem. 287, 1612\u20131619 (2007). https:\/\/doi.org\/10.1074\/jbc.R111.301150","DOI":"10.1074\/jbc.R111.301150"},{"key":"4","doi-asserted-by":"crossref","unstructured":"[4] Hofmann, K. P., Scheerer, P., Hildebrand, P. W., Choe, H-W., Park, J. H., Heck, M., et al. A G protein-coupled receptor at work: The rhodopsin model. Trends Biochem. Sci. 34, 540\u2013552 (2009). https:\/\/doi.org\/10.1016\/j.tibs.2009.07.005","DOI":"10.1016\/j.tibs.2009.07.005"},{"key":"5","doi-asserted-by":"crossref","unstructured":"[5] Haupts, U., Tittor, J., Oesterhelt, D. Closing in on bacteriorhodopsin: progress in understanding the molecule. Annu. Rev. Biophys. 28, 367\u2013399 (1999). https:\/\/doi.org\/10.1146\/annurev.biophys.28.1.367","DOI":"10.1146\/annurev.biophys.28.1.367"},{"key":"6","doi-asserted-by":"crossref","unstructured":"[6] Grote, M., Engelhard, M., Hegemann, P. Of ion pumps, sensors and channels\u2014perspectives on microbial rhodopsins between science and history. Biochim. Biophys. Acta Bioenerg. 1837, 533\u2013545 (2014). https:\/\/doi.org\/10.1016\/j.bbabio.2013.08.006","DOI":"10.1016\/j.bbabio.2013.08.006"},{"key":"7","doi-asserted-by":"crossref","unstructured":"[7] Govorunova, E. G., Sineshchekov, O. A., Li, H., Spudich, J. L. Microbial rhodopsins: Diversity, mechanisms, and optogenetic applications. Annu. Rev. Biochem. 86, 845\u2013872 (2017). https:\/\/doi.org\/10.1146\/annurev-biochem-101910-144233","DOI":"10.1146\/annurev-biochem-101910-144233"},{"key":"8","doi-asserted-by":"crossref","unstructured":"[8] Rozenberg, A., Inoue, K., Kandori, H., B\u00e9j\u00e0, O. Microbial rhodopsins: The last two decades. Annu. Rev. Microbiol. 75, 427\u2013447 (2021). https:\/\/doi.org\/10.1146\/annurev-micro-031721-020452","DOI":"10.1146\/annurev-micro-031721-020452"},{"key":"9","doi-asserted-by":"crossref","unstructured":"[9] Boyden, E. S., Zhang, F., Bamberg, E., Nagel, G., Deisseroth, K. Millisecond-timescale, genetically targeted optical control of neural activity. Nat. Neurosci. 8, 1263\u20131268 (2005). https:\/\/doi.org\/10.1038\/nn1525","DOI":"10.1038\/nn1525"},{"key":"10","doi-asserted-by":"crossref","unstructured":"[10] Deisseroth, K. Optogenetics. Nat. Methods 8, 26\u201329 (2011). https:\/\/doi.org\/10.1038\/nmeth.f.324","DOI":"10.1038\/nmeth.f.324"},{"key":"11","doi-asserted-by":"crossref","unstructured":"[11] Hegemann, P., M\u00f6glich, A. Channelrhodopsin engineering and exploration of new optogenetic tools. Nat. Methods 8, 39\u201342 (2011). https:\/\/doi.org\/10.1038\/nmeth.f.327","DOI":"10.1038\/nmeth.f.327"},{"key":"12","doi-asserted-by":"crossref","unstructured":"[12] Pushkarev, A., Inoue, K., Larom, S., Flores-Uribe, J., Singn, M., Konno, M., et al. A distinct abundant group of microbial rhodopsins discovered using functional metagenomics. Nature 558, 595\u2013599 (2018). https:\/\/doi.org\/10.1038\/s41586-018-0225-9","DOI":"10.1038\/s41586-018-0225-9"},{"key":"13","doi-asserted-by":"crossref","unstructured":"[13] Shihoya, W., Inoue, K., Singh, M., Konno, M., Hososhima, S., Yamashita, K., et al. Crystal structure of heliorhodopsin. Nature 574, 132\u2013136 (2019). https:\/\/doi.org\/10.1038\/s41586-019-1604-6","DOI":"10.1038\/s41586-019-1604-6"},{"key":"14","doi-asserted-by":"crossref","unstructured":"[14] Singh, M., Inoue, K., Pushkarev, A., B\u00e9j\u00e0, O., Kandori, H. Mutation study of heliorhodopsin 48C12. Biochemistry 57, 5041\u20135049 (2018). https:\/\/doi.org\/10.1021\/acs.biochem.8b00637","DOI":"10.1021\/acs.biochem.8b00637"},{"key":"15","doi-asserted-by":"crossref","unstructured":"[15] Shibukawa, A., Kojima, K., Nakajima, Y., Nishimura, Y., Yoshizawa, S., Sudo, Y. Photochemical characterization of a new heliorhodopsin from the Gram-negative eubacterium Bellilinea caldifistulae (BcHeR) and comparison with heliorhodopsin-48C12. Biochemistry 58, 2934\u20132943 (2019). https:\/\/doi.org\/10.1021\/acs.biochem.9b00257","DOI":"10.1021\/acs.biochem.9b00257"},{"key":"16","doi-asserted-by":"crossref","unstructured":"[16] Singh, M., Katayama, K., Beja, O., Kandori, H. Anion binding to mutants of the Schiff base counterion in heliorhodopsin 48C12. Phys. Chem. Chem. Phys. 21 23663\u201323671 (2019). https:\/\/doi.org\/10.1039\/c9cp04102h","DOI":"10.1039\/C9CP04102H"},{"key":"17","doi-asserted-by":"crossref","unstructured":"[17] Lu, Y., Zhou, X. E., Gao, X., Wang, N., Xia, R., Xu, Z., et al. Crystal structure of heliorhodopsin 48C12. Cell Res. 30, 88\u201390 (2020). https:\/\/doi.org\/10.1038\/s41422-019-0266-0","DOI":"10.1038\/s41422-019-0266-0"},{"key":"18","doi-asserted-by":"crossref","unstructured":"[18] Kovalev, K., Volkov, D., Astashkin, R., Alekseev, A., Gushchin, I., Haro-Moreno, J. M., et al. High-resolution structural insights into the heliorhodopsin family. Proc. Natl. Acad. Sci. U.S.A. 117, 4131\u20134141 (2020). https:\/\/doi.org\/10.1073\/pnas.1915888117","DOI":"10.1073\/pnas.1915888117"},{"key":"19","doi-asserted-by":"crossref","unstructured":"[19] Hashimoto, M., Katayama, K., Furutani, Y., Kandori, H. Zinc Binding to Heliorhodopsin. J Phys. Chem. Lett. 11, 8604\u20138609 (2020). https:\/\/doi.org\/10.1021\/acs.jpclett.0c02383","DOI":"10.1021\/acs.jpclett.0c02383"},{"key":"20","doi-asserted-by":"crossref","unstructured":"[20] Tanaka, T., Singh, M., Shihoya, W., Yamashita, K., Kandori, H., Nureki, O. Structural basis for unique color tuning mechanism in heliorhodopsin. Biochem. Biophys. Res. Commun. 533, 262\u2013267 (2020). https:\/\/doi.org\/10.1016\/j.bbrc.2020.06.124","DOI":"10.1016\/j.bbrc.2020.06.124"},{"key":"21","doi-asserted-by":"crossref","unstructured":"[21] Kim, S.-H., Chuon, K., Cho, S.-G., Choi, A., Meas, S., Cho, H.-S., et al. Color-tuning of natural variants of heliorhodopsin. Sci. Rep. 11, 854 (2021). https:\/\/doi.org\/10.1038\/s41598-020-72125-0","DOI":"10.1038\/s41598-020-72125-0"},{"key":"22","doi-asserted-by":"crossref","unstructured":"[22] Urui, T., Mizuno, M., Otomo, A., Kandori, H., Mizutani, Y. Resonance Raman determination of chromophore structures of heliorhodopsin photointermediates. J. Phys. Chem. B. 125, 7155\u20137162 (2021). https:\/\/doi.org\/10.1021\/acs.jpcb.1c04010","DOI":"10.1021\/acs.jpcb.1c04010"},{"key":"23","doi-asserted-by":"crossref","unstructured":"[23] Tomida, S., Kitagawa, S., Kandori, H., Furutani, Y. Inverse hydrogen-bonding change between the protonated retinal Schiff base and water molecules upon photoisomerization in heliorhodopsin 48C12. J. Phys. Chem. B 125, 8331\u20138341 (2021). https:\/\/doi.org\/10.1021\/acs.jpcb.1c01907","DOI":"10.1021\/acs.jpcb.1c01907"},{"key":"24","doi-asserted-by":"crossref","unstructured":"[24] Das, I., Pushkarev, A., Sheves, M. Light-induced conformational alterations in heliorhodopsin triggered by the retinal excited state. J. Phys. Chem. B 125, 8797\u20138804 (2021). https:\/\/doi.org\/10.1021\/acs.jpcb.1c04551","DOI":"10.1021\/acs.jpcb.1c04551"},{"key":"25","doi-asserted-by":"crossref","unstructured":"[25] Bulzu, P.-A., Kavagutti, V. S., Chiriac, M.-C., Vavourakis, C. D., Inoue, K., Kandori, H., et al. Heliorhodopsin evolution is driven by photosensory promiscuity in monoderms. mSphere 6, e0066121 (2021). https:\/\/doi.org\/10.1128\/mSphere.00661-21","DOI":"10.1128\/mSphere.00661-21"},{"key":"26","doi-asserted-by":"crossref","unstructured":"[26] Chazan, A., Rozenberg, A., Mannen, K., Nagata, T., Tahan, R., Yaish, S., et al. A. Diverse heliorhodopsins detected via functional metagenomics in freshwater Actinobacteria, Chloroflexi and Archaea. Environ. Microbiol. 24, 110\u2013121 (2022). https:\/\/doi.org\/10.1111\/1462-2920.15890","DOI":"10.1111\/1462-2920.15890"},{"key":"27","doi-asserted-by":"crossref","unstructured":"[27] Wijesiri, K., Gasc\u00f3n, J. A. Microsolvation effects in the spectral tuning of heliorhodopsin. J. Phys. Chem. B 126, 5803\u20135809 (2022). https:\/\/doi.org\/10.1021\/acs.jpcb.2c03672","DOI":"10.1021\/acs.jpcb.2c03672"},{"key":"28","doi-asserted-by":"crossref","unstructured":"[28] Besaw, J. E., Reichenwallner, J., De Guzman, P., Tucs, A., Kuo, A., Morizumi, T., et al. Low pH structure of heliorhodopsin reveals chloride binding site and intramolecular signaling pathway. Sci. Rep. 12, 13955 (2022). https:\/\/doi.org\/10.1038\/s41598-022-17716-9","DOI":"10.1038\/s41598-022-17716-9"},{"key":"29","doi-asserted-by":"crossref","unstructured":"[29] Urui, T., Das, I., Mizuno, M., Sheves, M., Mizutani, Y. Origin of a double-band feature in the ethylenic C=C stretching modes of the retinal chromophore in heliorhodopsins. J. Phys. Chem. B 126, 8680\u20138688 (2022). https:\/\/doi.org\/10.1021\/acs.jpcb.2c04883","DOI":"10.1021\/acs.jpcb.2c04883"},{"key":"30","doi-asserted-by":"crossref","unstructured":"[30] Tsujimura, M., Chiba, Y., Saito, K., Ishikita, H. Proton transfer and conformational changes along the hydrogen bond network in heliorhodopsin. Commun. Biol. 5, 1336 (2022). https:\/\/doi.org\/10.1038\/s42003-022-04311-x","DOI":"10.1038\/s42003-022-04311-x"},{"key":"31","doi-asserted-by":"crossref","unstructured":"[31] Hashimoto, M., Miyagawa, K., Singh, M., Katayama, K., Shoji, M., Furutani, Y., et al. Specific zinc binding to heliorhodopsin. Phys. Chem. Chem. Phys. 25, 3535\u20133543 (2023). https:\/\/doi.org\/10.1039\/d2cp04718g","DOI":"10.1039\/D2CP04718G"},{"key":"32","doi-asserted-by":"crossref","unstructured":"[32] Suzuki, S., Kumagai, S., Nagashima, T., Yamazaki, T., Okitsu, T., Wada, A., et al. Characterization of retinal chromophore and protonated Schiff base in Thermoplasmatales archaeon heliorhodopsin using solid-state NMR spectroscopy. Biophys. Chem. 296, 106991 (2023). https:\/\/doi.org\/10.1016\/j.bpc.2023.106991","DOI":"10.1016\/j.bpc.2023.106991"},{"key":"33","doi-asserted-by":"crossref","unstructured":"[33] Ganapathy, S., Meng, X., Mossel, D., Jagt, M., Brinks, D. Expanding the family of genetically encoded voltage indicators with a candidate Heliorhodopsin exhibiting near-infrared fluorescence. J. Biol. Chem. 299, 104771 (2023). https:\/\/doi.org\/10.1016\/j.jbc.2023.104771","DOI":"10.1016\/j.jbc.2023.104771"},{"key":"34","doi-asserted-by":"crossref","unstructured":"[34] Nakasone, Y., Kawasaki, Y., Konno, M., Inoue, K., Terazima, M. Time-resolved detection of light-induced conformational changes of heliorhodopsin. Phys. Chem. Chem. Phys. 25, 12833\u201312840 (2023). https:\/\/doi.org\/10.1039\/d3cp00711a","DOI":"10.1039\/D3CP00711A"},{"key":"35","doi-asserted-by":"crossref","unstructured":"[35] Chiba, Y., Tsujimura, M., Saito, K., Ishikita, H. pH-Dependent binding and releasing mechanism of acetate in the inner water cavity of heliorhodopsin. Biochemistry 62, 2363\u20132370 (2023). https:\/\/doi.org\/10.1021\/acs.biochem.3c00193","DOI":"10.1021\/acs.biochem.3c00193"},{"key":"36","doi-asserted-by":"crossref","unstructured":"[36] Singh, M., Hashimoto, M., Katayama, K., Furutani, Y., Kandori, H. Internal proton transfer in the activation of heliorhodopsin. J. Mol. Biol. 436, 168273 (2024). https:\/\/doi.org\/10.1016\/j.jmb.2023.168273","DOI":"10.1016\/j.jmb.2023.168273"},{"key":"37","doi-asserted-by":"crossref","unstructured":"[37] Palombo, R., Barneschi, L., Pedraza-Gonz\u00e1lez, L., Yang, X., Olivucci, M. Picosecond quantum-classical dynamics reveals that the coexistence of light-induced microbial and animal chromophore rotary motion modulates the isomerization quantum yield of heliorhodopsin. Phys. Chem. Chem. Phys. 26, 10343\u201310356 (2024). https:\/\/doi.org\/10.1039\/d4cp00193a","DOI":"10.1039\/D4CP00193A"},{"key":"38","doi-asserted-by":"crossref","unstructured":"[38] Fujimoto, K. J., Tsuzuki, Y. A., Inoue, K., Yanai, T. Molecular mechanisms behind circular dichroism spectral variations between channelrhodopsin and heliorhodopsin dimers. J. Phys. Chem. Lett. 15, 5788\u20135794 (2024). https:\/\/doi.org\/10.1021\/acs.jpclett.4c00879","DOI":"10.1021\/acs.jpclett.4c00879"},{"key":"39","doi-asserted-by":"crossref","unstructured":"[39] Wijesiri, K., Gasc\u00f3n, J. A. Structural models of the first molecular events in the heliorhodopsin photocycle. J. Phys. Chem. B 128, 5966\u20135972 (2024). https:\/\/doi.org\/10.1021\/acs.jpcb.4c00804","DOI":"10.1021\/acs.jpcb.4c00804"},{"key":"40","doi-asserted-by":"crossref","unstructured":"[40] Nakamura, T., Singh, M., Sugiura, M., Kato, S., Yamamoto, R., Kandori, H., et al. SNap Bond, a crucial hydrogen bond between Ser in helix 3 and Asn in helix 4, regulates the structural dynamics of heliorhodopsin. J. Mol. Biol. 436, 168666 (2024). https:\/\/doi.org\/10.1016\/j.jmb.2024.168666","DOI":"10.1016\/j.jmb.2024.168666"},{"key":"41","doi-asserted-by":"crossref","unstructured":"[41] Xia, R., Sun, M., Lu, Y., Wang, N., Zhang, A., Guo, C., et al. Cryo-EM structure of a nanobody-bound heliorhodopsin. Biochem. Biophys. Res. Commun. 750, 151398 (2025). https:\/\/doi.org\/10.1016\/j.bbrc.2025.151398","DOI":"10.1016\/j.bbrc.2025.151398"},{"key":"42","doi-asserted-by":"crossref","unstructured":"[42] Hososhima, S., Mizutori, R., Abe-Yoshizumi, R., Rozenberg, A., Shigemura, S., Pushkarev, A., et al. Proton-transporting heliorhodopsins from marine giant viruses. eLife 11, e78416 (2022). https:\/\/doi.org\/10.7554\/eLife.78416","DOI":"10.7554\/eLife.78416"},{"key":"43","doi-asserted-by":"crossref","unstructured":"[43] Cho, S.-G., Song, M., Chuon, K., Shim, J.-G., Meas, S., Jung, K.-H. Heliorhodopsin binds and regulates glutamine synthetase activity. PLoS Biol. 20, e3001817 (2022). https:\/\/doi.org\/10.1371\/journal.pbio.3001817","DOI":"10.1371\/journal.pbio.3001817"},{"key":"44","doi-asserted-by":"crossref","unstructured":"[44] Shim, J.-G., Cho, S.-G., Kim, S.-H., Chuon, K., Meas, S., Choi, A., et al. Heliorhodopsin helps photolyase to enhance the DNA repair capacity. Microbiol. Spectr. 10, e0221522 (2022). https:\/\/doi.org\/10.1128\/spectrum.02215-22","DOI":"10.1128\/spectrum.02215-22"},{"key":"45","doi-asserted-by":"crossref","unstructured":"[45] Cho, S.-G., Kim, J.-H., Lee, J.-E., Choi, I.-J., Song, M., Chuon, K., et al. Heliorhodopsin-mediated light-modulation of ABC transporter. Nat. Commun. 15, 4306 (2024). https:\/\/doi.org\/10.1038\/s41467-024-48650-1","DOI":"10.1038\/s41467-024-48650-1"},{"key":"46","doi-asserted-by":"crossref","unstructured":"[46] Thierstein, H. R., Young, J. R. Coccolithophores. in Springer. (Thierstein, H. R., Young, J. R. ed.) edi. num. 1, 565 pages (Springer-Verlag, Berlin and Heidelberg, 2004). https:\/\/doi.org\/10.1007\/978-3-662-06278-4","DOI":"10.1007\/978-3-662-06278-4"},{"key":"47","doi-asserted-by":"crossref","unstructured":"[47] Bidle, K. D., Haramaty, L., Barcelos, E., Ramos, J., Falkowski, P. Viral activation and recruitment of metacaspases in the unicellular coccolithophore, Emiliania huxleyi. Proc. Natl. Acad. Sci. U.S.A. 104, 6049\u20136054 (2007). https:\/\/doi.org\/10.1073\/pnas.0701240104","DOI":"10.1073\/pnas.0701240104"},{"key":"48","doi-asserted-by":"crossref","unstructured":"[48] Vardi, A., Van Mooy, B. A. S., Fredricks, H. F., Popendorf, K. J., Ossolinski, J. E., Haramaty, L., et al. Viral glycosphingolipids induce lytic infection and cell death in marine phytoplankton. Science 326, 861\u2013865 (2009). https:\/\/doi.org\/10.1126\/science.1177322","DOI":"10.1126\/science.1177322"},{"key":"49","doi-asserted-by":"crossref","unstructured":"[49] Chauhan, N., Dedman, C. J., Baldreki, C., Dowle, A. A., Larson, T. R., Rickaby, R. E. M. Contrasting species-specific stress response to environmental pH determines the fate of coccolithophores in future oceans. Mar. Pollut. Bull. 209, 117136 (2024). https:\/\/doi.org\/10.1016\/j.marpolbul.2024.117136","DOI":"10.1016\/j.marpolbul.2024.117136"},{"key":"50","doi-asserted-by":"crossref","unstructured":"[50] Kumar, S., Stecher, G., Suleski, M., Sanderford, M., Sharma, S., Tamura, K. MEGA12: molecular evolutionary genetic analysis version 12 for adaptive and green computing. Mol. Biol. Evol. 41, msac263 (2024). https:\/\/doi.org\/10.1093\/molbev\/msae263","DOI":"10.1093\/molbev\/msae263"},{"key":"51","doi-asserted-by":"crossref","unstructured":"[51] Saitou, N., Nei, M. The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406\u2013425 (1987). https:\/\/doi.org\/10.1093\/oxfordjournals.molbev.a040454","DOI":"10.1093\/oxfordjournals.molbev.a040454"},{"key":"52","doi-asserted-by":"crossref","unstructured":"[52] Felsenstein, J. Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39, 783\u2013791 (1985). https:\/\/doi.org\/10.1111\/j.1558-5646.1985.tb00420.x","DOI":"10.1111\/j.1558-5646.1985.tb00420.x"},{"key":"53","doi-asserted-by":"crossref","unstructured":"[53] Zuckerkandl, E., Pauling, L. Molecules as documents of evolutionary history. J. Theor. Biol. 8, 357\u2013366 (1965). https:\/\/doi.org\/10.1016\/0022-5193(65)90083-4","DOI":"10.1016\/0022-5193(65)90083-4"},{"key":"54","doi-asserted-by":"crossref","unstructured":"[54] Philosof, A., Yutin, N., Flores-Uribe, J., Sharon, I., Koonin, E. V., B\u00e9j\u00e0, O. Novel abundant oceanic viruses of uncultured marine group II Euryarchaeota. Curr. Biol. 27, 1362\u20131368 (2017). https:\/\/doi.org\/10.1016\/j.cub.2017.03.052","DOI":"10.1016\/j.cub.2017.03.052"},{"key":"55","doi-asserted-by":"crossref","unstructured":"[55] Yamauchi, Y., Konno, M., Ito, S., Tsunoda, S. P., Inoue, K., Kandori, H. Molecular properties of a DTD channelrhodopsin from Guillardia theta. Biophys. Physicobiol. 14, 57\u201366 (2017). https:\/\/doi.org\/10.2142\/biophysico.14.0_57","DOI":"10.2142\/biophysico.14.0_57"},{"key":"56","doi-asserted-by":"crossref","unstructured":"[56] Kawanabe, A., Furutani, Y., Jung, K.-H., Kandori, H. FTIR study of the photoisomerization processes in the 13-cis and all-trans forms of Anabaena sensory rhodopsin at 77 K. Biochemistry 45, 4362\u20134370 (2006). https:\/\/doi.org\/10.1021\/bi052324b","DOI":"10.1021\/bi052324b"},{"key":"57","doi-asserted-by":"crossref","unstructured":"[57] Kawanabe, A., Furutani, Y., Jung, K.-H., Kandori, H. Photochromism of Anabaena sensory rhodopsin. J. Am. Chem. Soc. 129, 8644\u20138649 (2007). https:\/\/doi.org\/10.1021\/ja072085a","DOI":"10.1021\/ja072085a"},{"key":"58","doi-asserted-by":"crossref","unstructured":"[58] Baasov, T., Friedman, N., Sheves, M. Factors affecting the C=N stretching in protonated retinal Schiff base: A model study for bacteriorhodopsin and visual pigments. 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