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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 and 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, vol.~282, No~2, p.~283-296. ISSN~1742-464X. Available from: https://dx.doi.org/10.1111/febs.13126.
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