The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F15%3A00080649" target="_blank" >RIV/00216224:14310/15:00080649 - isvavai.cz</a>
Výsledek na webu
<a href="http://onlinelibrary.wiley.com/doi/10.1111/febs.13126/abstract;jsessionid=0181D2471BC3A25A015704E9FAD26EE6.f01t04" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1111/febs.13126/abstract;jsessionid=0181D2471BC3A25A015704E9FAD26EE6.f01t04</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/febs.13126" target="_blank" >10.1111/febs.13126</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant
Popis výsledku v původním jazyce
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).
Název v anglickém jazyce
The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant
Popis výsledku anglicky
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).
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
—
Návaznosti výsledku
Projekt
<a href="/cs/project/GAP503%2F12%2F0369" target="_blank" >GAP503/12/0369: Nové flavin-dependentní enzymy Paracoccus denitrificans: reakční mechanismy, metabolické funkce a úloha v buněčném oxidačním stresu</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2015
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
FEBS Journal
ISSN
1742-464X
e-ISSN
—
Svazek periodika
282
Číslo periodika v rámci svazku
2
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
14
Strana od-do
283-296
Kód UT WoS článku
000348517400006
EID výsledku v databázi Scopus
—