Electron paramagnetic resonance power studies on the mixedvalence electron transfer centre of nitrous oxide reductase: presence of a modified CuA site in the enzyme from Pseudomonas stutzeri

1998 ◽  
Vol 95 (6) ◽  
pp. 1247-1253
Author(s):  
WILLIAM E. ANTHOLINE
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Transfer ◽  
Nitrous Oxide ◽  
Pseudomonas Stutzeri ◽  
Nitrous Oxide Reductase ◽  
Paramagnetic Resonance ◽  
Power Studies ◽  
Electron Paramagnetic

scholarly journals The NosX and NirX Proteins of Paracoccus denitrificans Are Functional Homologues: Their Role in Maturation of Nitrous Oxide Reductase

2000 ◽  
Vol 182 (18) ◽  
pp. 5211-5217 ◽  
Author(s):  
Neil F. W. Saunders ◽  
Jorrit J. Hornberg ◽  
Willem N. M. Reijnders ◽  
Hans V. Westerhoff ◽  
Simon de Vries ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Nitrous Oxide ◽  
Double Mutant ◽  
Paracoccus Denitrificans ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Resonance Spectroscopy ◽  
Nitrous Oxide Reductase ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic ◽  
Functional Homologues

ABSTRACT The nos (nitrous oxide reductase) operon ofParacoccus 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 CuA center. A twin-arginine motif in both NosX and NirX suggests that the NosX proteins are exported to the periplasm via the TAT translocon.

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