Inhibition of wheat leaf nitrate reductase activity by phenolic compounds.
Phenolic acids inhibited the activities of wheat leaf nitrate reductase depending on phenolic structure and concentration. Possible conformational change(s) in the enzyme induced by hydrogen bonding and/or hydrophobic interactions might be the cause of the enzyme inhibition. NADH:cytochrome C reductase partial activity was unaffected, which indicates that terminal nitrate-reducing domain of NR may be the site of polyphenol binding.
Albassam
B A
BA
Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia. bbassam@ksu.edu.sa
D002109:Caffeic Acids; D003373:Coumaric Acids; D004791:Enzyme Inhibitors / Q000378:metabolism; D047348:Hydrolyzable Tannins / Q000378:metabolism; D009245:NADH Dehydrogenase / Q000378:metabolism; D050895:Nitrate Reductase (NADH); D009565:Nitrate Reductases / Q000037:antagonists & inhibitors*; D010636:Phenols / Q000378:metabolism; D018515:Plant Leaves / Q000201:enzymology; D011422:Propionates; D014908:Triticum / Q000201:enzymology*; D014641:Vanillic Acid
D002109:Caffeic Acids; D003373:Coumaric Acids; D004791:Enzyme Inhibitors; D047348:Hydrolyzable Tannins; D010636:Phenols; D011422:Propionates; D009245:NADH Dehydrogenase; D009565:Nitrate Reductases; D050895:Nitrate Reductase (NADH); D014641:Vanillic Acid; C495469:p-coumaric acid; C040048:caffeic acid