Zobrazeno 1 - 10
of 28
pro vyhledávání: '"T. Y. Fufina"'
Autor:
L. G. Vasilieva, T. Y. Fufina
Publikováno v:
Biochemistry (Moscow). 86:517-524
Photosynthetic reaction center (RC) of the purple bacterium Rhodobacter sphaeroides is one of the most well-studied transmembrane pigment-protein complexes. It is a relatively stable protein with established conditions for its isolation from membrane
Autor:
L. G. Vasilieva, Vladimir A. Shuvalov, Anatoly Ya. Shkuropatov, I. I. Proskuryakov, Alexey A. Zabelin, A. M. Khristin, T. Y. Fufina, R. A. Khatypov
Publikováno v:
Photosynthesis Research. 146:109-121
In photosynthetic reaction centers (RCs) of purple bacteria, conserved histidine residues [His L173 and His M202 in Rhodobacter (Rba.) sphaeroides] are known to serve as fifth axial ligands to the central Mg atom of the bacteriochlorophyll (BChl) mol
Autor:
Kõu Timpmann, Arvi Freiberg, Azat Gabdulkhakov, Kristjan Leiger, A. A. Ashikhmin, Juha Linnanto, T. Y. Fufina, Margus Rätsep, Andrey A. Moskalenko
Publikováno v:
The Journal of Physical Chemistry B. 123:29-38
As a basis of photosynthesis, photoinduced oxidation of (bacterio)chlorophyll molecules in the special reaction center complexes has been a subject of extensive research. In contrast, the generally harmful photooxidation of antenna chromoproteins has
Publikováno v:
Biochemistry (Moscow). 80:647-653
In the bacterial photosynthetic reaction center (RC), asymmetric protein environment of the bacteriochlorophyll (BChl) dimer largely determines the photophysical and photochemical properties of the primary electron donor. Previously, we noticed signi
Publikováno v:
Biochemistry (Moscow). 75:208-213
We demonstrated earlier that as a result of the I(L177)H mutation in the photosynthetic reaction center (RC) of the bacterium Rhodobacter sphaeroides, one of the bacteriochlorophylls (BChl) binds with the L-subunit, simultaneously raising coordinatio
Autor:
M.G. Zvereva, A.Y. Shkuropatov, L. G. Vasilieva, V. A. Shkuropatova, Alexey A. Zabelin, Vladimir A. Shuvalov, T. Y. Fufina
Publikováno v:
Biochemistry (Moscow). 74:68-74
Methods of photoinduced Fourier transform infrared (FTIR) difference spectroscopy and circular dichroism were employed for studying features of pigment-protein interactions caused by replacement of isoleucine L177 by histidine in the reaction center
Publikováno v:
Photosynthesis research. 125(1-2)
New histidine residue was introduced in M196 position in the reaction center of Rhodobacter sphaeroides in order to alter polarity of the BChl dimer’s protein environment and to study how it affects properties and structure of the primary electron
The electron and proton transport mediated by protein-bound cofactors in photosynthesis have been investigated by various methods in order to determine the energetics, the dynamics and the pathway of this process. In purple bacteria, primary photosyn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2ae7570232d7e0cea0f98f5433e0b28
https://europepmc.org/articles/PMC3660888/
https://europepmc.org/articles/PMC3660888/
Publikováno v:
Advanced Topics in Science and Technology in China ISBN: 9783642320330
In the reaction center of purple bacterium Rhodobacter sphaeroides histidine L173 serves as the fifth ligand of Mg atom of the bacteriochlorophyll PA. It is known that after substitution of this histidine by leucine the bacteriochlorophyll loses its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5c945c8253cb9cfd68f6aacacfd6dd27
https://doi.org/10.1007/978-3-642-32034-7_9
https://doi.org/10.1007/978-3-642-32034-7_9
Publikováno v:
FEBS letters. 581(30)
In this work, we report the unique case of bacteriochlorophyll (BChl) – protein covalent attachment in a photosynthetic membrane complex caused by a single mutation. The isoleucine L177 was substituted by histidine in the photosynthetic reaction ce