About: Heterologous expression and molecular characterization of the NAD(P)H: acceptor oxidoreductase (FerB) of Paracoccus denitrificans

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About: Heterologous expression and molecular characterization of the NAD(P)H: acceptor oxidoreductase (FerB) of Paracoccus denitrificans Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

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rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	FerB is a flavoenzyme capable of reducing quinones, ferric complexes and chromate. Its expression in E. coli as a hexahistidine fusion resulted in a functional product only when the tag was placed on the C-terminus. The molecular mass values estimated by GPC were compatible with the existence of either dimer or trimer, whereas the light scattering data, together with cross-linking experiments that yielded exclusively monomer and dimer bands on SDS-PAGE, strongly supported a dimeric nature of both native and tagged form of FerB. These two proteins also exhibited almost identical secondary structure as judged by Fourier transform infra red spectrometry. The presence of tag, however, shifted the temperature of thermal inactivation as well as the thermal denaturation curve towards lower temperatures. Despite somewhat lower thermal stability, the fusion protein is considered a better candidate for crystallization than the wild-type one due to a more negative value of its second optical virial coefficient. FerB is a flavoenzyme capable of reducing quinones, ferric complexes and chromate. Its expression in E. coli as a hexahistidine fusion resulted in a functional product only when the tag was placed on the C-terminus. The molecular mass values estimated by GPC were compatible with the existence of either dimer or trimer, whereas the light scattering data, together with cross-linking experiments that yielded exclusively monomer and dimer bands on SDS-PAGE, strongly supported a dimeric nature of both native and tagged form of FerB. These two proteins also exhibited almost identical secondary structure as judged by Fourier transform infra red spectrometry. The presence of tag, however, shifted the temperature of thermal inactivation as well as the thermal denaturation curve towards lower temperatures. Despite somewhat lower thermal stability, the fusion protein is considered a better candidate for crystallization than the wild-type one due to a more negative value of its second optical virial coefficient. (en)
Title	Heterologous expression and molecular characterization of the NAD(P)H: acceptor oxidoreductase (FerB) of Paracoccus denitrificans Heterologous expression and molecular characterization of the NAD(P)H: acceptor oxidoreductase (FerB) of Paracoccus denitrificans (en)
skos:prefLabel	Heterologous expression and molecular characterization of the NAD(P)H: acceptor oxidoreductase (FerB) of Paracoccus denitrificans Heterologous expression and molecular characterization of the NAD(P)H: acceptor oxidoreductase (FerB) of Paracoccus denitrificans (en)
skos:notation	RIV/00027162:_____/09:#0000543!RIV10-MZE-00027162
http://linked.open...avai/riv/aktivita	P Z
http://linked.open...avai/riv/aktivity	P(GA525/07/1069), Z(MSM0021622413), Z(MZE0002716202)
http://linked.open...iv/cisloPeriodika	2
http://linked.open...vai/riv/dodaniDat	2010
http://linked.open...aciTvurceVysledku	Plocková, Jana Tesařík, Radek Turánek, Jaroslav
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	Výzkumný ústav veterinárního lékařství, v.v.i.
http://linked.open...dnocenehoVysledku	317053
http://linked.open...ai/riv/idVysledku	RIV/00027162:_____/09:#0000543
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Quinone reductase; Protein expression in E. coli; His-tag fusion; Light scattering; Cross-linking; FT-IR spectrometry; Differential scanning calorimetry; Thermal inactivation (en)
http://linked.open.../riv/klicoveSlovo	Light scattering Cross-linking Differential scanning calorimetry FT-IR spectrometry His-tag fusion Protein expression in E. coli Quinone reductase Thermal inactivation
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[7DC43BE70308]
http://linked.open...i/riv/nazevZdroje	Protein Expression and Purification
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	3 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (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	68
http://linked.open...iv/tvurceVysledku	Wimmerová, M. Turánek, Jaroslav Tesařík, Radek Plocková, Jana Kučera, I. Sedláček, V.
http://linked.open...ain/vavai/riv/wos	000272103000016
http://linked.open...n/vavai/riv/zamer	Proteiny v metabolismu a při interakci organismů s prostředím Animal disease research, prevention and food chain protection
issn	1046-5928
number of pages	6 (xsd:int)

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