Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
19138657
DOI
10.1016/j.abb.2008.12.016
PII: S0003-9861(08)00588-2
Knihovny.cz E-resources
- MeSH
- Genes, Bacterial MeSH
- Quinones metabolism MeSH
- DNA, Bacterial genetics MeSH
- FMN Reductase antagonists & inhibitors chemistry genetics metabolism MeSH
- Enzyme Inhibitors chemistry pharmacology MeSH
- Kinetics MeSH
- Molecular Sequence Data MeSH
- Mutation MeSH
- NAD(P)H Dehydrogenase (Quinone) antagonists & inhibitors chemistry genetics metabolism MeSH
- Paracoccus denitrificans enzymology genetics MeSH
- Promoter Regions, Genetic MeSH
- Recombinant Fusion Proteins antagonists & inhibitors chemistry genetics metabolism MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Substrate Specificity MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Quinones MeSH
- DNA, Bacterial MeSH
- ferric citrate iron reductase MeSH Browser
- FMN Reductase MeSH
- Enzyme Inhibitors MeSH
- NAD(P)H Dehydrogenase (Quinone) MeSH
- Recombinant Fusion Proteins MeSH
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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