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Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78394

Messerschmidt,  A.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;
Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Einsle, O., Stach, P., Messerschmidt, A., Klimmek, O., Simon, J., Kröger, A., et al. (2002). Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes. Acta Crystallographica Section D - Biological Crystallography, 58, 341-342.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6FCA-4
Zusammenfassung
Crystals of the complex between the enzyme cytochrome c nitrite reductase (NrfA) and the membrane-bound quinol oxidase and electron carrier NrfH were grown by vapour diffusion using ammonium sulfate as a precipitant. In the epsilon- proteobacterium Wolinella succinogenes, NrfA and NrfH form a functional membrane-bound complex which catalyzes the last step in the metabolic pathway of nitrate dissimilation. NrfH represents a prototype of a large family of putative bacterial quinol oxidases, the NapC/NirT family, which have been proposed to serve as electron donors for a variety of reductases. Crystal growth of the NrfHA complex was strongly dependent on the presence of detergent; the crystals grown belonged to space group I422.