About: The Structural and Functional Basis of Catalysis Mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans

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About: The Structural and Functional Basis of Catalysis Mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans Goto Sponge NotDistinct Permalink

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Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0096262
Description	FerB from Paracoccus denitrificans is a soluble cytoplasmic flavoprotein that accepts redox equivalents from NADH or NADPH and transfers them to various acceptors such as quinones, ferric complexes and chromate. The crystal structure and small-angle X-ray scattering measurements in solution reported here reveal a head-to-tail dimer with two flavin mononucleotide groups bound at the opposite sides of the subunit interface. The dimers tend to self-associate to a tetrameric form at higher protein concentrations. Amino acid residues important for the binding of FMN and NADH and for the catalytic activity are identified and verified by site-directed mutagenesis. In particular, we show that Glu77 anchors a conserved water molecule in close proximity to the O2 of FMN, with the probable role of facilitating flavin reduction. Hydride transfer is shown to occur from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring. FerB from Paracoccus denitrificans is a soluble cytoplasmic flavoprotein that accepts redox equivalents from NADH or NADPH and transfers them to various acceptors such as quinones, ferric complexes and chromate. The crystal structure and small-angle X-ray scattering measurements in solution reported here reveal a head-to-tail dimer with two flavin mononucleotide groups bound at the opposite sides of the subunit interface. The dimers tend to self-associate to a tetrameric form at higher protein concentrations. Amino acid residues important for the binding of FMN and NADH and for the catalytic activity are identified and verified by site-directed mutagenesis. In particular, we show that Glu77 anchors a conserved water molecule in close proximity to the O2 of FMN, with the probable role of facilitating flavin reduction. Hydride transfer is shown to occur from the 4-pro-S position of NADH to the solvent-accessible si side of the flavin ring. (en)
Title	The Structural and Functional Basis of Catalysis Mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans The Structural and Functional Basis of Catalysis Mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans (en)
skos:prefLabel	The Structural and Functional Basis of Catalysis Mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans The Structural and Functional Basis of Catalysis Mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans (en)
skos:notation	RIV/00216224:14310/14:00073680!RIV15-MSM-14310___
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(EE2.3.30.0037), P(GAP503/12/0369), P(GPP503/10/P217)
http://linked.open...iv/cisloPeriodika	5
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Kučera, Igor Marek, Jaromír Sedláček, Vojtěch Klumpler, Tomáš
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	47819
http://linked.open...ai/riv/idVysledku	RIV/00216224:14310/14:00073680
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	enzyme; flavin; crystal structure; mechanism (en)
http://linked.open.../riv/klicoveSlovo	flavin crystal structure enzyme mechanism
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[1ECF0FAFAB26]
http://linked.open...i/riv/nazevZdroje	PLOS ONE
http://linked.open...in/vavai/riv/obor	CE
http://linked.open...ichTvurcuVysledku	4 (xsd:int)
http://linked.open...cetTvurcuVysledku	4 (xsd:int)
http://linked.open...vavai/riv/projekt	Employment of Best Young Scientists for International Cooperation Empowerment Electron transfer reactions in the bacterial flavoenzyme FerB: molecular mechanisms, evolutionary aspects and enzyme engineering Novel flavin-dependent enzymes of Paracoccus denitrificans: reaction mechanisms, metabolic functions and their role in cellular oxidative stress
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	9
http://linked.open...iv/tvurceVysledku	Marek, Jaromír Kučera, Igor Sedláček, Vojtěch Klumpler, Tomáš
http://linked.open...ain/vavai/riv/wos	000336838000029
issn	1932-6203
number of pages	13 (xsd:int)
http://bibframe.org/vocab/doi	10.1371/journal.pone.0096262
http://localhost/t...ganizacniJednotka	14310

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