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

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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
Citation
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.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Molecular basis of cell and tissue regulations Structure, function and regulation of FerB, a broad-specificity bacterial oxidoreductase of a potential ecotechnological relevance Molecular mechanisms of the cell proliferation and differentiation