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; SEDLÁČEK Vojtěch; MAREK Jaromír; WIMMEROVÁ Michaela; KUČERA Igor
• Year of publication: 2010
• Type: Article in Periodical
• Magazine / Source: Acta crystallographica. Section F Structural biology and crystallization communications
• MU Faculty or unit: Faculty of Science
• Web: http://www3.interscience.wiley.com/journal/123345936/abstract
• Field: Biochemistry
• Keywords: PSEUDOMONAS-PUTIDA; QUINONE REDUCTASE; FERRIC REDUCTASE; FLAVOPROTEINS; CRYSTALS; PROTEIN
• Description: 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.

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