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@article{1218633, author = {Sedláček, Vojtěch and Ptáčková, Nikola and Rejmontová, Petra and Kučera, Igor}, article_number = {2}, doi = {http://dx.doi.org/10.1111/febs.13126}, keywords = {flavoprotein; oxidative stress; Paracoccus denitrificans; superoxide; ubiquinone}, language = {eng}, issn = {1742-464X}, journal = {FEBS Journal}, title = {The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant}, url = {http://onlinelibrary.wiley.com/doi/10.1111/febs.13126/abstract;jsessionid=0181D2471BC3A25A015704E9FAD26EE6.f01t04}, volume = {282}, year = {2015} }
TY - JOUR ID - 1218633 AU - Sedláček, Vojtěch - Ptáčková, Nikola - Rejmontová, Petra - Kučera, Igor PY - 2015 TI - The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant JF - FEBS Journal VL - 282 IS - 2 SP - 283-296 EP - 283-296 PB - WILEY-BLACKWELL SN - 1742464X KW - flavoprotein KW - oxidative stress KW - Paracoccus denitrificans KW - superoxide KW - ubiquinone UR - http://onlinelibrary.wiley.com/doi/10.1111/febs.13126/abstract;jsessionid=0181D2471BC3A25A015704E9FAD26EE6.f01t04 L2 - http://onlinelibrary.wiley.com/doi/10.1111/febs.13126/abstract;jsessionid=0181D2471BC3A25A015704E9FAD26EE6.f01t04 N2 - 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. ER -
SEDLÁČEK, Vojtěch, Nikola PTÁČKOVÁ, Petra REJMONTOVÁ a Igor KUČERA. The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant. \textit{FEBS Journal}. WILEY-BLACKWELL, 2015, roč.~282, č.~2, s.~283-296. ISSN~1742-464X. Dostupné z: https://dx.doi.org/10.1111/febs.13126.
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