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

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 ɛ‐proteobacterium Wolinella succinogenes, NrfA and NrfH form a functional me...

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Veröffentlicht in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-02, Vol.58 (2), p.341-342
Hauptverfasser: Einsle, Oliver, Stach, Petra, Messerschmidt, Albrecht, Klimmek, Oliver, Simon, Jörg, Kröger, Achim, Kroneck, Peter M. H.
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Sprache:eng
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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 ɛ‐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.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S090744490102039X