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

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About: Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans Goto Sponge NotDistinct Permalink

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	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. 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. (en)
Title	Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans (en)
skos:prefLabel	Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans (en)
skos:notation	RIV/00216224:14310/09:00029290!RIV10-MSM-14310___
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA525/07/1069), Z(MSM0021622413)
http://linked.open...iv/cisloPeriodika	1
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Kučera, Igor Sedláček, Vojtěch
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Masarykova univerzita / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	306802
http://linked.open...ai/riv/idVysledku	RIV/00216224:14310/09:00029290
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	NADH; Flavoprotein; Quinone reduction; Redox cycling (en)
http://linked.open.../riv/klicoveSlovo	NADH Flavoprotein Quinone reduction Redox cycling
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[205A79B2637E]
http://linked.open...i/riv/nazevZdroje	Archives of biochemistry and biophysics
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	3 (xsd:int)
http://linked.open...vavai/riv/projekt	Structure, function and regulation of FerB, a broad-specificity bacterial oxidoreductase of a potential ecotechnological relevance
http://linked.open...UplatneniVysledku	2009
http://linked.open...v/svazekPeriodika	483
http://linked.open...iv/tvurceVysledku	Kučera, Igor Sedláček, Vojtěch van Spanning, Rob
http://linked.open...n/vavai/riv/zamer	Proteiny v metabolismu a při interakci organismů s prostředím
issn	0003-9861
number of pages	8 (xsd:int)
http://localhost/t...ganizacniJednotka	14310

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