Low-temperature Raman spectroscopy of sodium-pump rhodopsin from <i>Indibacter alkaliphilus</i>: insight of Na<sup>+</sup> binding for active Na<sup>+</sup> transport

Physical Chemistry Chemical Physics - Tập 23 Số 3 - Trang 2072-2079
Yushi Nakamizo1,2,3,4,5, Tomotsumi Fujisawa1,2,3,4,5, Takashi Kikukawa6,7,8,3,9, Akiko Okamura6,10,3,9, Hiroaki Baba1,2,3,4,5, Masashi Unno1,2,3,4,5
1Department of Chemistry and Applied Chemistry, Faculty of Science and Engineering, Saga University, Saga 840-8502, Japan
2Faculty of Science and Engineering
3Japan
4Saga 840-8502
5saga University
6Faculty of Advanced Life Science, Hokkaido University, Sapporo 060-0810, Japan
7Global Station for Soft Matter
8Global Station for Soft Matter, Global Institution for Collaborative Research and Education, Hokkaido University, Sapporo 060-0810, Japan
9Sapporo 060-0810
10Hokkaido University

Tóm tắt

We carried out the low-temperature Raman measurement of a sodium pump rhodopsin from Indibacter alkaliphilus with/without Na+ to examine the structural change for the light-driven Na+ pump.

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Tài liệu tham khảo

Govorunova, 2017, Annu. Rev. Biochem., 86, 845, 10.1146/annurev-biochem-101910-144233

Ernst, 2014, Chem. Rev., 114, 126, 10.1021/cr4003769

Kandori, 2015, Front. Mol. Biosci., 2, 52, 10.3389/fmolb.2015.00052

Schneider, 2015, Annu. Rev. Biophys., 44, 167, 10.1146/annurev-biophys-060414-034014

Inoue, 2014, Biochim. Biophys. Acta, 1837, 562, 10.1016/j.bbabio.2013.05.005

Inoue, 2013, Nat. Commun., 4, 1678, 10.1038/ncomms2689

Kwon, 2013, Genome Biol. Evol., 5, 187, 10.1093/gbe/evs134

Kato, 2016, BioEssays, 38, 1274, 10.1002/bies.201600065

Inoue, 2015, Trends Microbiol., 23, 91, 10.1016/j.tim.2014.10.009

Inoue, 2019, Nat. Commun., 10, 1993, 10.1038/s41467-019-10000-x

Hoque, 2016, PLoS One, 11, e0166820, 10.1371/journal.pone.0166820

Nogly, 2015, Nat. Struct. Mol. Biol., 22, 351, 10.1038/nsmb.3017

Kajimoto, 2017, J. Phys. Chem. B, 121, 4431, 10.1021/acs.jpcb.7b02421

Tahara, 2015, J. Phys. Chem. Lett., 6, 4481, 10.1021/acs.jpclett.5b01994

Tsunoda, 2017, PLoS One, 12, e0179232, 10.1371/journal.pone.0179232

Balashov, 2014, Biochemistry, 53, 7549, 10.1021/bi501064n

Nishimura, 2019, J. Phys. Chem. B, 123, 3430, 10.1021/acs.jpcb.9b00928

Hontani, 2016, Phys. Chem. Chem. Phys., 18, 24729, 10.1039/C6CP05240A

Chen, 2018, Phys. Chem. Chem. Phys., 20, 17694, 10.1039/C8CP02599A

Murabe, 2020, J. Am. Chem. Soc., 142, 16023, 10.1021/jacs.0c07264

Kovalev, 2019, Sci. Adv., 5, eaav2671, 10.1126/sciadv.aav2671

Inoue, 2015, Angew. Chem., Int. Ed., 54, 11536, 10.1002/anie.201504549

Kovalev, 2020, Nat. Commun., 11, 2137, 10.1038/s41467-020-16032-y

Skopintsev, 2020, Nature, 583, 314, 10.1038/s41586-020-2307-8

Gushchin, 2016, FEBS J., 283, 1232, 10.1111/febs.13585

Kato, 2015, Nature, 521, 48, 10.1038/nature14322

Gushchin, 2015, Nat. Struct. Mol. Biol., 22, 390, 10.1038/nsmb.3002

Shibata, 2018, Sci. Rep., 8, 8262, 10.1038/s41598-018-26606-y

Engelhard, 2018, Chem. Rev., 118, 10629, 10.1021/acs.chemrev.7b00715

Fujisawa, 2019, Biochemistry, 58, 4159, 10.1021/acs.biochem.9b00643

Fujisawa, 2018, FEBS Lett., 592, 3054, 10.1002/1873-3468.13219

Li, 2015, Biophys. J., 109, 1446, 10.1016/j.bpj.2015.08.018

Lozier, 1975, Biophys. J., 15, 955, 10.1016/S0006-3495(75)85875-9

Smith, 1987, J. Am. Chem. Soc., 109, 3108, 10.1021/ja00244a038

Smith, 1987, J. Phys. Chem., 91, 804, 10.1021/j100288a011

Otomo, 2020, Biochemistry, 59, 520, 10.1021/acs.biochem.9b01062

Matsuo, 2020, J. Phys. Chem. Lett., 11, 8579, 10.1021/acs.jpclett.0c02448

Braiman, 1982, Proc. Natl. Acad. Sci. U. S. A., 79, 403, 10.1073/pnas.79.2.403

Maeda, 1991, Photochem. Photobiol., 54, 911, 10.1111/j.1751-1097.1991.tb02111.x

Furutani, 2006, Biochemistry, 45, 11836, 10.1021/bi0610597

M. S. Braiman , Methods in Enzymology , Academic Press , 1986 , vol. 127, pp. 587–597

Eyring, 1980, Biochemistry, 19, 2410, 10.1021/bi00552a020

Haraguchi, 2018, Proc. Natl. Acad. Sci. U. S. A., 115, 8671, 10.1073/pnas.1806491115

Otomo, 2018, J. Phys. Chem. Lett., 9, 6431, 10.1021/acs.jpclett.8b02741

Aton, 1977, Biochemistry, 16, 2995, 10.1021/bi00632a029

van den Berg, 1990, Biophys. J., 58, 135, 10.1016/S0006-3495(90)82359-6

Kato, 2015, J. Phys. Chem. Lett., 6, 5111, 10.1021/acs.jpclett.5b02371

Ono, 2014, J. Phys. Chem. B, 118, 4784, 10.1021/jp500756f

Ito, 2018, J. Phys. Chem. B, 122, 165, 10.1021/acs.jpcb.7b11064

Suomivuori, 2017, Proc. Natl. Acad. Sci. U. S. A., 114, 7043, 10.1073/pnas.1703625114