Einsle, O. ; Stach, P. ; Messerschmidt, A. ; Klimmek, O. ; Simon, J. ; Kröger, A. ; Kroneck, P. M. H. (2002):
Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes.
In: Acta crystallographica. Section D, Biological crystallography, 58 (Pt 2), pp. 341-2. ISSN 0907-4449,
[Article]
Abstract
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.
| Item Type: | Article |
|---|---|
| Erschienen: | 2002 |
| Creators: | Einsle, O. ; Stach, P. ; Messerschmidt, A. ; Klimmek, O. ; Simon, J. ; Kröger, A. ; Kroneck, P. M. H. |
| Title: | Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes. |
| Language: | English |
| Abstract: | 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. |
| Journal or Publication Title: | Acta crystallographica. Section D, Biological crystallography |
| Volume of the journal: | 58 |
| Issue Number: | Pt 2 |
| Divisions: | 10 Department of Biology > Microbial Energy Conversion and Biotechnology ?? fb10_mikrobiologie ?? 10 Department of Biology |
| Date Deposited: | 07 Dec 2010 15:12 |
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