Application of direct electrometry in studies of microbial rhodopsins reconstituted in proteoliposomes
Author:
Funder
Russian Scientific Foundation
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology,Biophysics
Link
https://link.springer.com/content/pdf/10.1007/s12551-022-00986-y.pdf
Reference48 articles.
1. Balashov SP (2000) Protonation reactions and their coupling in bacteriorhodopsin. Biochim Biophys Acta (BBA)-Bioenergetics 1460:75–94. https://doi.org/10.1016/S0005-2728(00)00131-6
2. Balashov SP, Petrovskaya LE, Lukashev EP, Imasheva ES, Dioumaev AK, Wang JM et al (2012) Aspartate-histidine interaction in the retinal schiff base counterion of the light-driven proton pump of Exiguobacterium sibiricum. Biochemistry 51:5748–5762. https://doi.org/10.1021/bi300409m
3. Balashov SP, Petrovskaya LE, Imasheva ES, Lukashev EP, Dioumaev AK, Wang JM et al (2013) Breaking the carboxyl rule: lysine 96 facilitates reprotonation of the Schiff base in the photocycle of a retinal protein from Exiguobacterium sibiricum. J Biol Chem 288:21254–21265. https://doi.org/10.1074/jbc.M113.465138
4. Balashov SP, Imasheva ES, Dioumaev AK, Wang JM, Jung K-H, Lanyi JK (2014) Light-driven Na+ pump from Gillisia limnaea: a high-affinity Na+ binding site is formed transiently in the photocycle. Biochemistry 53:7549–7561. https://doi.org/10.1021/bi501064n
5. Berndt A, Lee SY, Wietek J, Ramakrishnan C, Steinberg EE, Rashid AJ et al (2016) Structural foundations of optogenetics: Determinants of channelrhodopsin ion selectivity. Proc Natl Acad Sci USA 113:822–829. https://doi.org/10.1073/pnas.1523341113
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