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

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.

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Genre: Journal Article
Alternative Title : Acta Crystallogr. Sect. D-Biol. Crystallogr.

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 Creators:
Einsle, O., Author
Stach, P., Author
Messerschmidt, A.1, 2, Author           
Klimmek, O., Author
Simon, J., Author
Kröger, A., Author
Kroneck, P. M. H., Author
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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 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.

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Language(s): eng - English
 Dates: 2002-02
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 35336
ISI: 000173442200029
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Title: Acta Crystallographica Section D - Biological Crystallography
  Alternative Title : Acta Crystallogr. Sect. D-Biol. Crystallogr.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 58 Sequence Number: - Start / End Page: 341 - 342 Identifier: ISSN: 0907-4449