scholarly journals Kinetic studies of the induction of nitrate reductase and cytochrome c reductase in the fungus Aspergillus nidulans

1967 ◽  
Vol 104 (3) ◽  
pp. 1033-1039 ◽  
Author(s):  
DJ Cove
Keyword(s):  
Cytochrome C ◽  
Nitrate Reductase ◽  
Aspergillus Nidulans ◽  
Kinetic Studies ◽  
Cytochrome C Reductase

scholarly journals Structural and functional relationships of enzyme activities induced by nitrate in barley

1970 ◽  
Vol 119 (4) ◽  
pp. 715-725 ◽  
Author(s):  
John L. Wray ◽  
Philip Filner
Keyword(s):  
Cytochrome C ◽  
Nitrate Reductase ◽  
Nitrate Reductase Activity ◽  
Reductase Activity ◽  
Bottom Layer ◽  
Sucrose Density Gradient ◽  
Enzyme Complex ◽  
Cytochrome C Reductase ◽  
Functional Relationships ◽  
Nadh Cytochrome

1. Nitrate induces the development of NADH-nitrate reductase (EC 1.6.6.1), FMNH2–nitrate reductase and NADH–cytochrome c reductase activities in barley shoots. 2. Sucrose-density-gradient analysis shows one band of NADH–nitrate reductase (8S), one band of FMNH2–nitrate reductase activity (8S) and three bands of NADH–cytochrome c reductase activity (bottom layer, 8S and 3.7S). Both 8S and 3.7S NADH–cytochrome c reductase activities are inducible by nitrate, but the induction of the 8S band is much more marked. 3. The 8S NADH–cytochrome c reductase band co-sediments with both NADH–nitrate reductase activity and FMNH2–nitrate reductase activity. Nitrite reductase activity (4.6S) did not coincide with the activity of either the 8S or the 3.7S NADH–cytochrome c reductase. 4. FMNH2–nitrate reductase activity is more stable (t½ 12.5min) than either NADH–nitrate reductase activity (t½ 0.5min) or total NADH–cytochrome c reductase activity (t½ 1.5min) at 45°C. 5. NADH–cytochrome c reductase and NADH–nitrate reductase activities are more sensitive to p-chloromercuribenzoate than is FMNH2–nitrate reductase activity. 6. Tungstate prevents the formation of NADH–nitrate reductase and FMNH2–nitrate reductase activities, but it causes superinduction of NADH–cytochrome c reductase activity. Molybdate overcomes the effects of tungstate. 7. The same three bands (bottom layer, 8S and 3.7S) of NADH–cytochrome c reductase activity are observed irrespective of whether induction is carried out in the presence or absence of tungstate, but only the activities in the 8S and 3.7S bands are increased. 8. The results support the idea that NADH–nitrate reductase, FMNH2–nitrate reductase and NADH–cytochrome c reductase are activities of the same enzyme complex, and that in the presence of tungstate the 8S enzyme complex is formed but is functional only with respect to NADH–cytochrome c reductase activity.

Nature of cytochrome C reductase in nitrate reductase-deficient mutants in barley

1983 ◽  
Vol 190 (2) ◽  
pp. 222-226 ◽  
Author(s):  
Komaratchi R. Narayanan ◽  
David A. Somers ◽  
Andris Kleinhofs ◽  
Robert L. Warner
Keyword(s):  
Cytochrome C ◽  
Nitrate Reductase ◽  
Cytochrome C Reductase

scholarly journals Nitrate Reductase and Soluble Cytochrome c Reductase(s) in Higher Plants

1978 ◽  
Vol 61 (5) ◽  
pp. 748-752 ◽  
Author(s):  
William Wallace ◽  
Christopher B. Johnson
Keyword(s):  
Cytochrome C ◽  
Nitrate Reductase ◽  
Higher Plants ◽  
Cytochrome C Reductase
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