Crystallization and initial X-ray diffraction studies of the flavoenzyme NAD(P)H:(acceptor) oxidoreductase (FerB) from the soil bacterium Paracoccus denitrificans

KLUMPLER, Tomáš, Vojtěch SEDLÁČEK, Jaromír MAREK, Michaela WIMMEROVÁ and Igor KUČERA. Crystallization and initial X-ray diffraction studies of the flavoenzyme NAD(P)H:(acceptor) oxidoreductase (FerB) from the soil bacterium Paracoccus denitrificans. Acta crystallographica. Section F Structural biology and crystallization communications. Malden, USA: WILEY-BLACKWELL PUBLISHING, INC, 2010, F66, No 4, p. 431-434. ISSN 1744-3091.

Basic information

• Original name: Crystallization and initial X-ray diffraction studies of the flavoenzyme NAD(P)H:(acceptor) oxidoreductase (FerB) from the soil bacterium Paracoccus denitrificans
• Authors: KLUMPLER, Tomáš (203 Czech Republic), Vojtěch SEDLÁČEK (203 Czech Republic), Jaromír MAREK (203 Czech Republic, guarantor), Michaela WIMMEROVÁ (203 Czech Republic) and Igor KUČERA (203 Czech Republic).
• Edition: Acta crystallographica. Section F Structural biology and crystallization communications, Malden, USA, WILEY-BLACKWELL PUBLISHING, INC, 2010, 1744-3091.

Other information

• Original 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
• WWW: URL
• Impact factor: Impact factor: 0.563
• RIV identification code: RIV/00216224:14310/10:00044021
• Organization unit: Faculty of Science
• UT WoS: 000276488700013
• Keywords (in Czech): flavoproteiny; krystal; reduktázy
• Keywords in English: PSEUDOMONAS-PUTIDA; QUINONE REDUCTASE; FERRIC REDUCTASE; FLAVOPROTEINS; CRYSTALS; PROTEIN
• Tags: International impact, Reviewed

Abstract

The flavin-dependent enzyme FerB from Paracoccus denitrificans reduces a broad range of compounds, including ferric complexes, chromate and most notably quinones, at the expense of the reduced nicotinamide adenine dinucleotide cofactors NADH or NADPH. Recombinant unmodified and SeMet-substituted FerB were crystallized under similar conditions by the hanging-drop vapour-diffusion method with microseeding using PEG 4000 as the precipitant. FerB crystallized in several different crystal forms, some of which diffracted to approximately 1.8 A resolution. Structure determination by the three-wavelength MAD/MRSAD method is now in progress.

Links

• GA525/07/1069, research and development project: Name: Struktura, funkce a regulace FerB, širokospecifické bakteriální oxidoreduktasy s možným významem pro ekotechnologii

Investor: Czech Science Foundation, Structure, function and regulation of FerB, a broad-specificity bacterial oxidoreductase of a potential ecotechnological relevance

• GD204/08/H054, research and development project: Name: Molekulární mechanismy proliferace a diferenciace buněk

Investor: Czech Science Foundation, Molecular mechanisms of the cell proliferation and differentiation

• MSM0021622413, plan (intention): Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

• MSM0021622415, plan (intention): Name: Molekulární podstata buněčných a tkáňových regulací

Investor: Ministry of Education, Youth and Sports of the CR, Molecular basis of cell and tissue regulations