The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
The flavoprotein FerB of Paracoccus denitrificans binds to membranes, reduces ubiquinone and superoxide, and acts as in vivo antioxidant
Original language 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).
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP503%2F12%2F0369" target="_blank" >GAP503/12/0369: Novel flavin-dependent enzymes of Paracoccus denitrificans: reaction mechanisms, metabolic functions and their role in cellular oxidative stress</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEBS Journal
ISSN
1742-464X
e-ISSN
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Volume of the periodical
282
Issue of the periodical within the volume
2
Country of publishing house
US - UNITED STATES
Number of pages
14
Pages from-to
283-296
UT code for WoS article
000348517400006
EID of the result in the Scopus database
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