2009
Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans
SEDLÁČEK, Vojtěch; Rob VAN SPANNING and Igor KUČERABasic information
Original name
Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans
Name in Czech
Charakterizace chinonreduktasové aktivity FerB proteinu z bakterie Paracoccus denitrificans
Authors
SEDLÁČEK, Vojtěch (203 Czech Republic, guarantor); Rob VAN SPANNING (528 Netherlands) and Igor KUČERA (203 Czech Republic)
Edition
Archives of biochemistry and biophysics, New York, Academic Press, 2009, 0003-9861
Other information
Language
English
Type of outcome
Article in a journal
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
is not subject to a state or trade secret
Impact factor
Impact factor: 3.046
RIV identification code
RIV/00216224:14310/09:00029290
Organization unit
Faculty of Science
UT WoS
000263854400005
Keywords in English
NADH; Flavoprotein; Quinone reduction; Redox cycling
Tags
International impact, Reviewed
Changed: 19/5/2009 13:24, Mgr. Vojtěch Sedláček, Ph.D.
In the original language
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.
In Czech
FerB protein z bakterie Paracoccus denitrificans vykazuje aktivitu NAD(P)H:Fe(III)chelát, chromát a chinon oxidoreduktas. Sekvenční analýza řadí FerB do rodiny rozpustných flavin obsahujících chinonreduktas. Enzym redukuje různé chinonové substráty jako 1,4-benzochinon, 1,2- naftochinon a 1,4-naftochinon kinetikou ping-pongového mechnismu. Dikumarol a cibakron 3GA jsou kompetitivními inhibitory k oxidujícímu NADH. V případě benzochinonů, FerB patrně přenáší dva elektrony současně, kdežto v případě naftochinonů probíhá jednoelektronová redukce projevující se ve tvorbě semichinonových radikálů. Kmen mutantní ve ferB vykazoval zvýšenou rezistenci k 1,4-naftochinonu, naznačující absenci FerB-mediovaného redoxního cyklu. Promotor ferB vykazoval vysokou bazální aktivitu během celého růstu P. denitrificans, která nebyla dále zesilována přítomností různých naftochinonů. Toto naznačilo, že ferB je exprimován konstitutivně.
Links
| GA525/07/1069, research and development project |
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| MSM0021622413, plan (intention) |
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