The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant

Investor logo

Warning

This publication doesn't include Faculty of Education. It includes Faculty of Science. Official publication website can be found on muni.cz.
Authors

SEDLÁČEK Vojtěch PTÁČKOVÁ Nikola REJMONTOVÁ Petra KUČERA Igor

Year of publication 2015
Type Article in Periodical
Magazine / Source FEBS Journal
MU Faculty or unit

Faculty of Science

Citation
Web http://onlinelibrary.wiley.com/doi/10.1111/febs.13126/abstract;jsessionid=0181D2471BC3A25A015704E9FAD26EE6.f01t04
Doi http://dx.doi.org/10.1111/febs.13126
Field Biochemistry
Keywords flavoprotein; oxidative stress; Paracoccus denitrificans; superoxide; ubiquinone
Description 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.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.