Characterization of membrane-bound nitrate reductase from denitrifying bacteriaOchrobactrum anthropi SY509

2006 ◽  
Vol 11 (1) ◽  
pp. 32-37 ◽  
Author(s):  
Seung Hwan Kim ◽  
Seung Hoon Song ◽  
Yong Je Yoo
2008 ◽  
Vol 13 (8) ◽  
pp. 1321-1333 ◽  
Author(s):  
Cristina Correia ◽  
Stéphane Besson ◽  
Carlos D. Brondino ◽  
Pablo J. González ◽  
Guy Fauque ◽  
...  

FEBS Letters ◽  
1978 ◽  
Vol 95 (2) ◽  
pp. 290-294 ◽  
Author(s):  
Gérard Giordano ◽  
Alec Graham ◽  
David H. Boxer ◽  
Bruce A. Haddock ◽  
Edgard Azoulay

2001 ◽  
Vol 67 (11) ◽  
pp. 5122-5126 ◽  
Author(s):  
Monique Sabaty ◽  
Cécile Avazeri ◽  
David Pignol ◽  
André Vermeglio

ABSTRACT Preliminary studies showed that the periplasmic nitrate reductase (Nap) of Rhodobacter sphaeroides and the membrane-bound nitrate reductases of Escherichia coli are able to reduce selenate and tellurite in vitro with benzyl viologen as an electron donor. In the present study, we found that this is a general feature of denitrifiers. Both the periplasmic and membrane-bound nitrate reductases of Ralstonia eutropha, Paracoccus denitrificans, and Paracoccus pantotrophus can utilize potassium selenate and potassium tellurite as electron acceptors. In order to characterize these reactions, the periplasmic nitrate reductase of R. sphaeroides f. sp. denitrificans IL106 was histidine tagged and purified. The V max andKm were determined for nitrate, tellurite, and selenate. For nitrate, values of 39 μmol · min−1 · mg−1 and 0.12 mM were obtained for V max and Km , respectively, whereas the V max values for tellurite and selenate were 40- and 140-fold lower, respectively. These low activities can explain the observation that depletion of the nitrate reductase in R. sphaeroides does not modify the MIC of tellurite for this organism.


FEBS Letters ◽  
1996 ◽  
Vol 392 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Manuel Fernández-López ◽  
José Olivares ◽  
Eulogio J. Bedmar

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