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JOURNALS // Mendeleev Communications // Archive
Mendeleev Commun., 2018 Volume 28, Issue 4, Pages 406–408 (Mi mendc1782)
This article is cited in 2 papers

Communications

The effect of the chromophoric group modification on the optical properties of retinal proteins

N. E. Belikova, I. A. Melnikovaa, O. V. Deminaa, L. E. Petrovskayab, E. A. Kryukovab, D. A. Dolgikhb, P. K. Kuzmichevc, V. V. Chupinc, A. Yu. Lukind, A. N. Shumskya, I. Chizhove, P. P. Levina, M. P. Kirpichnikovb, S. D. Varfolomeeva, A. A. Khodonova

a N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russian Federation
b M.M. Shemyakin–Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation
c Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, Moscow Region, Russian Federation
d M.V. Lomonosov Institute of Fine Chemical Technologies, MIREA - Russian Technological University, Moscow, Russian Federation
e Institute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany

Abstract: The effects of chromophoric group structures on the functional properties of bacteriorhodopsin (BR) and proteorhodopsin from E. sibiricum (ESRh) were compared. ESRh retinal binding site was found as preserving the similar stereo- and spatial restrictions on the chromophore structure during the retinal protein reconstitution process (except for C25-analog AR8). It was revealed that the structure peculiarities of the chromophore analog molecules affect the optical parameters of ESRh and BR pigment families in similar ways.

Language: English

DOI: 10.1016/j.mencom.2018.07.022


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