Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans

Archives of Biochemistry and Biophysics
Vojtech SedlácekIgor Kucera

Abstract

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.

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Citations

Jun 19, 2009·Extremophiles : Life Under Extreme Conditions·Rob Uche OnyenwokeJuergen Wiegel
Apr 13, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Tomás KlumplerIgor Kucera
Jul 2, 2010·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Timothy S MagnusonDavid E Cummings
Aug 10, 2016·The Journal of Biological Chemistry·Jacob BallGiovanni Gadda

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