| Autor: |
Saunders NF; Department of Molecular Cell Physiology, Faculty of Biology, BioCentrum Amsterdam, Vrije Universiteit, Amsterdam, The Netherlands., Hornberg JJ, Reijnders WN, Westerhoff HV, de Vries S, van Spanning RJ |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of bacteriology [J Bacteriol] 2000 Sep; Vol. 182 (18), pp. 5211-7. |
| DOI: |
10.1128/JB.182.18.5211-5217.2000 |
| Abstrakt: |
The nos (nitrous oxide reductase) operon of Paracoccus denitrificans contains a nosX gene homologous to those found in the nos operons of other denitrifiers. NosX is also homologous to NirX, which is so far unique to P. denitrificans. Single mutations of these genes did not result in any apparent phenotype, but a double nosX nirX mutant was unable to reduce nitrous oxide. Promoter-lacZ assays and immunoblotting against nitrous oxide reductase showed that the defect was not due to failure of expression of nosZ, the structural gene for nitrous oxide reductase. Electron paramagnetic resonance spectroscopy showed that nitrous oxide reductase in cells of the double mutant lacked the Cu(A) center. A twin-arginine motif in both NosX and NirX suggests that the NosX proteins are exported to the periplasm via the TAT translocon. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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