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Identification of key proteins involved in the anammox reaction

Roger Karlsson ; Anders Karlsson (Institutionen för mikroteknologi och nanovetenskap) ; Ola Bäckman ; Bengt R Johansson ; Stefan Hulth
FEMS microbiology letters (1574-6968). Vol. 297 (2009), 1, p. 87-94.
[Artikel, refereegranskad vetenskaplig]

Bacteria performing anaerobic ammonium oxidation (anammox) are key players in the global nitrogen cycle due to their inherent ability to convert biologically available nitrogen to N(2). Anammox is increasingly being exploited during wastewater treatment worldwide, and about 50% of the total N(2) production in marine environments is estimated to proceed by the anammox pathway. To fully understand the microbial functionality and mechanisms that control environmental feedbacks of the anammox reaction, key proteins involved in the reaction must be identified. In this study we have utilized an analytical protocol that facilitates detection of proteins associated with the anammoxosome, an intracellular membrane compartment within the anammox bacterium. The protocol enabled us to identify several key proteins of the anammox reaction including a hydrazine hydrolase producing hydrazine, a hydrazine-oxidizing enzyme converting hydrazine to N(2) and a membrane-bound ATP synthase generating ATP from the gradients of protons formed in the anammox reaction. We also performed immunogold labelling electron microscopy to determine the subcellular location of the hydrazine hydrolase. The results from our study support the hypothesis that proteins associated with the anammoxosome host the complete suite of reactions during anammox.



Denna post skapades 2009-11-10. Senast ändrad 2016-10-10.
CPL Pubid: 101466

 

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Institutioner (Chalmers)

Institutionen för kemi (2001-2011)
Institutionen för mikroteknologi och nanovetenskap
Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi (GU)

Ämnesområden

Kemi
Biologiska vetenskaper

Chalmers infrastruktur