Detailed Information on Publication Record
2015
The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant
SEDLÁČEK, Vojtěch, Nikola PTÁČKOVÁ, Petra REJMONTOVÁ and Igor KUČERABasic information
Original name
The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant
Name in Czech
Flavoprotein FerB z Paracoccus denitrificans se váže na membrány, redukuje ubichinon a superoxid a působí jako antioxidant in vivo
Authors
SEDLÁČEK, Vojtěch (203 Czech Republic, belonging to the institution), Nikola PTÁČKOVÁ (203 Czech Republic, belonging to the institution), Petra REJMONTOVÁ (203 Czech Republic, belonging to the institution) and Igor KUČERA (203 Czech Republic, guarantor, belonging to the institution)
Edition
FEBS Journal, WILEY-BLACKWELL, 2015, 1742-464X
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 4.237
RIV identification code
RIV/00216224:14310/15:00080649
Organization unit
Faculty of Science
UT WoS
000348517400006
Keywords (in Czech)
flavoprotein; oxidační stres; Paracoccus denitrificans; superoxid; ubichinon
Keywords in English
flavoprotein; oxidative stress; Paracoccus denitrificans; superoxide; ubiquinone
Tags
International impact, Reviewed
Změněno: 20/7/2019 14:16, prof. RNDr. Igor Kučera, DrSc.
V originále
FerB is a flavin mononucleotide (FMN)-containing NAD(P)H:acceptor oxidoreductase of unknown function that is found in the cytoplasm of the bacterium Paracoccus denitrificans. Based on measurements of fluorescence anisotropy, we report here that recombinant FerB readily binds to artificial membrane vesicles. If ubiquinone is incorporated into the membrane, FerB catalyzes its conversion to ubihydroquinone, which may be followed fluorimetrically (with ferricyanide and pyranine entrapped inside the liposomes) or by HPLC. FerB also reduces exogenously added superoxide or superoxide that has been enzymatically generated by the xanthine/xanthine oxidase system or P. denitrificans membrane vesicles. In whole cells, deficiency of FerB increases sensitivity to methyl viologen, as indicated by a lower growth rate and increased production of reactive aldehydes (by-products of lipid oxidation). Taken together, these data support a role for FerB in protection of cells against lipid peroxidation-mediated oxidative stress, and suggest that FerB is a prokaryotic counterpart of mammalian NAD(P)H:quinone oxidoreductase 1.
In Czech
FerB je NAD(P)H:akceptor oxidoreduktasa s neznámou funkcí, která se nachází v cytoplazmě bakterie Paracoccus denitrificans. Měřením anizotropie fluorescence jsme zjistili, že se FerB váže na membránové váčky. Je-li do membrány zabudován ubichinon, FerB katalyzuje jeho přeměnu na ubihydrochinon, jež může být sledována fluorimetricky (s ferrikyanidem a pyraninem uzavřeným uvnitř váčků). FerB rovněž redukuje exogenní superoxid nebo superoxid generovaný enzymově systémem xanthin/xanthin oxidasa nebo váčky z cytoplazmatické membrány P. denitrificans. U celých buněk defekt FerB zvyšuje citlivost k methylviologenu, jež se projevuje nižší růstovou rychlostí a zvýšenou produkcí reaktivních aldehydů (produktů oxidace lipidů). V souhrnu výsledky svědčí o úloze FerB při ochraně buněk před oxidačním stresem a ukazují, že FerB je prokaryontní obdoba savčí NAD(P)H:chinon oxidoreduktasy 1.
Links
| GAP503/12/0369, research and development project |
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