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@article{832280,
author = {Sedláček, Vojtěch and van Spanning, Rob and Kučera, Igor},
article_location = {New York},
article_number = {1},
keywords = {NADH; Flavoprotein; Quinone reduction; Redox cycling},
language = {eng},
issn = {0003-9861},
journal = {Archives of biochemistry and biophysics},
title = {Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans},
volume = {483},
year = {2009}
}
TY - JOUR
ID - 832280
AU - Sedláček, Vojtěch - van Spanning, Rob - Kučera, Igor
PY - 2009
TI - Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans
JF - Archives of biochemistry and biophysics
VL - 483
IS - 1
SP - 29-36
EP - 29-36
PB - Academic Press
SN - 00039861
KW - NADH
KW - Flavoprotein
KW - Quinone reduction
KW - Redox cycling
N2 - The ferric reductase B (FerB) protein of Paracoccus denitrificans exhibits activity of an NAD(P)H: Fe(III) chelate, chromate and quinone oxidoreductase. Sequence analysis places FerB in a family of soluble flavin-containing quinone reductases. The enzyme reduces a range of quinone substrates, including derivatives of 1,4-benzoquinone and 1,2- and 1,4-naphthoquinone, via a ping-pong kinetic mechanism. Dicoumarol and Cibacron Blue 3GA are competitive inhibitors of NADH oxidation. In the case of benzoquinones, FerB apparently acts through a two-electron transfer process, whereas in the case of naphthoquinones, one-electron reduction takes place resulting in the formation of semiquinone radicals. A ferB mutant strain exhibited an increased resistance to 1,4-naphthoquinone, attributable to the absence of the FerB-mediated redox cycling. The ferB promoter displayed a high basal activity throughout the growth of P. denitrificans, which could not be further enhanced by addition of different types of naphthoquinones. This indicates that the ferB gene is expressed constitutively.
ER -
SEDLÁČEK, Vojtěch, Rob VAN SPANNING and Igor KUČERA. Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans. \textit{Archives of biochemistry and biophysics}. New York: Academic Press, 2009, vol.~483, No~1, p.~29-36. ISSN~0003-9861.
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