EFFECT OF SUBSTRATE ON THE CATALYTIC ACTIVITY AND STABILITY OF NITRATE REDUCTASE FROM RHIZOBIUM MELILOTI

1981 ◽  
Vol 9 (2) ◽  
pp. 322P-322P
Author(s):  
Marianna Telegdi
1973 ◽  
Vol 246 (153) ◽  
pp. 153-154 ◽  
Author(s):  
Á. KONDOROSI ◽  
ILONA BARABÁS ◽  
ZÓRA SVÁB ◽  
L. OROSZ ◽  
T. SIK ◽  
...  

1980 ◽  
Vol 35 (9-10) ◽  
pp. 702-707 ◽  
Author(s):  
Candadai S. Ramadoss

Abstract The inhibition of the activity of xanthine oxidase by vanadate was strikingly similar to vanadate inhibition of another molybdoprotein nitrate reductase. Although the main catalytic activity of both enzymes was inhibited, the partial NADH oxidase activity associated with these enzymes was stimulated several fold. It appears that the metal ion binds at multiple site in both enzymes. In the absence of any enzymes a combination of vanadium (V) and molybdenum (V) in air was found to oxide NADH rapidly.


1980 ◽  
Vol 60 (1) ◽  
pp. 209-212 ◽  
Author(s):  
H. ANTOUN ◽  
L. M. BORDELEAU ◽  
D. PRÉVOST ◽  
R. A. LACHANCE

Specific activities of the assimilatory and "regulatory" types of nitrate reductase were studied in 41 strains of Rhizobium meliloti having different symbiotic nitrogen fixation activities. Both nitrate reductase enzymes were present in very effective and ineffective strains and no significant correlation was found between the specific activities of the two enzymes and the dry matter yields of alfalfa obtained with the 41 strains. Measurements of the specific activities of the two nitrate reductase enzymes in the vegetative bacteria cannot be used as a rapid physiological test for the selection of very effective strains of R. meliloti.


1979 ◽  
Vol 25 (3) ◽  
pp. 298-301 ◽  
Author(s):  
Ilona Barabás ◽  
Tibor Sik

In two out of three pleiotropic mutants of Rhizobium meliloti, defective in nitrate reductase induced by amino acid utilization in vegetative bacteria and in symbiotic nitrogen fixation, nitrogenase activity could be restored completely by purines and partially by the amino acids L-glutamate, L-aspartate, L-glutamine, and L-asparagine. The compounds restoring effectiveness in nitrogen fixation did not restore nitrate reductase activity in vegetative bacteria. The restoration of effectiveness supports our earlier conclusion that the mutation is not in the structural gene for a suggested common subunit of nitrogenase and nitrate reductase.


Biochemistry ◽  
2010 ◽  
Vol 49 (11) ◽  
pp. 2424-2432 ◽  
Author(s):  
Vincent Fourmond ◽  
Bénédicte Burlat ◽  
Sébastien Dementin ◽  
Monique Sabaty ◽  
Pascal Arnoux ◽  
...  

1989 ◽  
Vol 135 (2) ◽  
pp. 207-211 ◽  
Author(s):  
Cesáreo Arrese-Igor ◽  
José M. Estavillo ◽  
José I. Peña ◽  
Carmen Gonzalez-Murua ◽  
Pedro M. Aparicio-Tejo

Sign in / Sign up

Export Citation Format

Share Document