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

Warning

This publication doesn't include Faculty of Arts. It includes Faculty of Science. Official publication website can be found on muni.cz.

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