Zobrazeno 1 - 10
of 43
pro vyhledávání: '"Yulia V, Bertsova"'
Publikováno v:
Biochemistry (Moscow). 87:731-741
This review provides a brief description of the structure and transport function of the recently discovered family of retinal-containing Na+-translocating rhodopsins. The main emphasis is put on the kinetics of generation of electric potential differ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::049c97f343041fa5dfb5fa02c5259e73
https://doi.org/10.1134/s0006297922080053
https://doi.org/10.1134/s0006297922080053
Autor:
Yulia V. Bertsova, Marina V. Serebryakova, Victor A. Anashkin, Alexander A. Baykov, Alexander V. Bogachev
Genes of putative reductases of α,β-unsaturated carboxylic acids are abundant among anaerobic and facultatively anaerobic microorganisms, yet substrate specificity has been experimentally verified for few encoded proteins. Here, we co-produced inEs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9396f186081283402a4c4ebe2d1a96e2
https://doi.org/10.1101/2023.03.04.531086
https://doi.org/10.1101/2023.03.04.531086
Publikováno v:
FEMS Microbiology Letters. 368
Azotobacter vinelandii, the model microbe in nitrogen fixation studies, uses the ferredoxin:NAD+-oxidoreductase Rnf to regenerate ferredoxin (flavodoxin), acting as an electron donor for nitrogenase. However, the relative contribution of Rnf to nitro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a977f68e5e91107ec89bf0733ef7318
https://doi.org/10.1093/femsle/fnab130
https://doi.org/10.1093/femsle/fnab130
Autor:
Alexander A. Baykov, Leonid V. Kulik, Alexander V. Bogachev, Mahir D. Mamedov, Yulia V. Bertsova
Publikováno v:
Photosynthesis Research. 142:127-136
Flavodoxins are small proteins with a non-covalently bound FMN that can accept two electrons and accordingly adopt three redox states: oxidized (quinone), one-electron reduced (semiquinone), and two-electron reduced (quinol). In iron-deficient cyanob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65e3b490f6a4a7fd95e995fe2b8e3dd7
https://doi.org/10.1007/s11120-019-00658-1
https://doi.org/10.1007/s11120-019-00658-1
Publikováno v:
FEMS microbiology letters. 367(20)
The cytoplasmic fumarate reductase of Klebsiella pneumoniae (FRD) is a monomeric protein which contains three prosthetic groups: noncovalently bound FMN and FAD plus a covalently bound FMN. In the present work, NADH is revealed to be an inherent elec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::293bc842dd8c5bb98341e286d8afc5d9
https://pubmed.ncbi.nlm.nih.gov/33107907
https://pubmed.ncbi.nlm.nih.gov/33107907
Publikováno v:
Biochemical Society Transactions. 46:1161-1169
Flavins, cofactors of many enzymes, are often covalently linked to these enzymes; for instance, flavin adenine mononucleotide (FMN) can form a covalent bond through either its phosphate or isoalloxazine group. The prevailing view had long been that a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b006b124916c81f282eebc7aeb7f1b9
https://doi.org/10.1042/bst20180524
https://doi.org/10.1042/bst20180524
Publikováno v:
Journal of Inorganic Biochemistry. 184:15-18
A paramagnetic Cys4[Fe] center was detected by pulse EPR in Na+-translocating NADH:quinone-oxidoreductase (Na+-NQR) by influence of this center on transverse and longitudinal spin relaxation of Na+-NQR flavin radicals. The oxidation state of the Cys4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d5f02866056aeec367382f1aa99d29fe
https://doi.org/10.1016/j.jinorgbio.2018.04.004
https://doi.org/10.1016/j.jinorgbio.2018.04.004
Identification of the key determinant of the transport promiscuity in Na + -translocating rhodopsins
Autor:
Viktor A. Anashkin, Yulia V. Bertsova, Alexander A. Baykov, Alexander V. Bogachev, Mahir D. Mamedov, Adalyat M. Mamedov
Publikováno v:
Biochemical and Biophysical Research Communications. 499:600-604
Bacterial Na+-transporting rhodopsins convert solar energy into transmembrane ion potential difference. Typically, they are strictly specific for Na+, but some can additionally transport H+. To determine the structural basis of cation promiscuity in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a71bc60a54567fdb5e9465b7490ba1ab
https://doi.org/10.1016/j.bbrc.2018.03.196
https://doi.org/10.1016/j.bbrc.2018.03.196
Autor:
Alexander A. Baykov, Mahir D. Mamedov, Alexander M. Arutyunyan, Viktor A. Anashkin, Alexander V. Bogachev, Adalyat M. Mamedov, Yulia V. Bertsova
Publikováno v:
Photosynthesis Research. 136:161-169
Light-driven H+, Cl- and Na+ rhodopsin pumps all use a covalently bound retinal molecule to capture light energy. Some H+-pumping rhodopsins (xanthorhodopsins; XRs) additionally contain a carotenoid antenna for light absorption. Comparison of the ava
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6103be3cdf007db0e0027773274effa0
https://doi.org/10.1007/s11120-017-0453-0
https://doi.org/10.1007/s11120-017-0453-0
Publikováno v:
Biochemistry. Biokhimiia. 84(11)
Genomes of photoautotrophic organisms containing type I photosynthetic reaction center were searched for the rnf genes encoding Na+-translocating ferredoxin:NAD+ oxidoreductase (RNF). These genes were absent in heliobacteria, cyanobacteria, algae, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4c21dadb6fdff81ae3c02420792e60e
https://pubmed.ncbi.nlm.nih.gov/31760926
https://pubmed.ncbi.nlm.nih.gov/31760926