Structure/function study of photoreceptive proteins by FTIR spectroscopy

H Kandori - Bulletin of the Chemical Society of Japan, 2020 - academic.oup.com
Light-induced difference Fourier-transform infrared (FTIR) spectroscopy is a powerful,
sensitive and informative method for studying protein structural changes in photoreceptive …

Molecular mechanism of light-driven sodium pum**

K Kovalev, R Astashkin, I Gushchin, P Orekhov… - Nature …, 2020 - nature.com
The light-driven sodium-pum** rhodopsin KR2 from Krokinobacter eikastus is the only
non-proton cation active transporter with demonstrated potential for optogenetics. However …

Structure and mechanisms of sodium-pum** KR2 rhodopsin

K Kovalev, V Polovinkin, I Gushchin, A Alekseev… - Science …, 2019 - science.org
Rhodopsins are the most universal biological light-energy transducers and abundant
phototrophic mechanisms that evolved on Earth and have a remarkable diversity and …

Characterization of retinal chromophore and protonated Schiff base in Thermoplasmatales archaeon heliorhodopsin using solid-state NMR spectroscopy

S Suzuki, S Kumagai, T Nagashima, T Yamazaki… - Biophysical …, 2023 - Elsevier
Heliorhodopsin (HeR) is a seven-helical transmembrane protein with a retinal chromophore
that corresponds to a new rhodopsin family. HeR from the archaebacterium …

Solid-state NMR analysis of the sodium pump Krokinobacter rhodopsin 2 and its H30A mutant

J Kaur, CN Kriebel, P Eberhardt, O Jakdetchai… - Journal of structural …, 2019 - Elsevier
Abstract Krokinobacter eikastus rhodopsin 2 (KR2) is a pentameric, light-driven ion pump,
which selectively transports sodium or protons. The mechanism of ion selectivity and transfer …

Structural and functional consequences of the H180A mutation of the light-driven sodium pump KR2

CN Kriebel, M Asido, J Kaur, J Orth, P Braun… - Biophysical …, 2023 - cell.com
Abstract Krokinobacter eikastus rhodopsin 2 (KR2) is a light-driven pentameric sodium
pump. Its ability to translocate cations other than protons and to create an electrochemical …

Allosteric communication with the retinal chromophore upon ion binding in a light-driven sodium ion-pum** rhodopsin

A Otomo, M Mizuno, K Inoue, H Kandori… - Biochemistry, 2019 - ACS Publications
Krokinobacter rhodopsin 2 (KR2) serves as a light-driven sodium ion pump in the presence
of sodium ion and works as a proton pump in the presence of larger monovalent cations …

Probing the photointermediates of light-driven sodium ion pump KR2 by DNP-enhanced solid-state NMR

O Jakdetchai, P Eberhardt, M Asido, J Kaur… - Science …, 2021 - science.org
The functional mechanism of the light-driven sodium pump Krokinobacter eikastus
rhodopsin 2 (KR2) raises fundamental questions since the transfer of cations must differ from …

Real-time identification of two substrate-binding intermediates for the light-driven sodium pump rhodopsin

T Kato, T Tsukamoto, M Demura, T Kikukawa - Journal of Biological …, 2021 - ASBMB
Membrane transport proteins undergo critical conformational changes during substrate
uptake and release, as the substrate-binding site is believed to switch its accessibility from …

[HTML][HTML] Solid-state NMR of the retinal protonated Schiff base in microbial rhodopsins

S Kumagai, I Kawamura - Magnetic Resonance Letters, 2024 - Elsevier
Rhodopsin is a seven-helical transmembrane protein with a retinal chromophore covalently
bound to a conserved lysine in helix G via a retinal protonated Schiff base (RPSB). Microbial …