title: Molybdenum nutrition of isolates of four Aspergillus species.
abstract: The molybdenum requirement for growth and conidial formation by Aspergillus flavus, A. terreus, and A. sulphureus was found to be 0.2 ppb, which was one-fifth that of an A. niger isolate. Molybdenum deficiency depressed growth, conidial formation, dry weight, soluble protein, and the specific activities of nitrate reductase, succinic dehydrogenase, and aconitase in all the isolates of Aspergillus studied, but the specific activities of catalase and peroxidase were depressed only in isolates of A. niger, A. terreus, and A. flavus. Also, molybdenum deficiency stimulated the specific activities of acid phosphatase and ribonuclease in the A. flavus isolate, although the specific activities of these enzymes decreased in other isolates. Eighteen hours after the addition of molybdenum (5 ppb) to molybdenum-deficient (0.02 ppb) cultures of A. niger, the specific activities of catalase, peroxidase and succinic dehydrogenase were restored in the absence of cycloheximide, while the specific activity of nitrate reductase was recovered even in the presence of the inhibitor. There was no effect on the specific activities of aconitase and acid phosphatase following the addition of molybdenum to molybdenum-deficient cultures of A. niger.
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism; D000154:Aconitate Hydratase / Q000378:metabolism; D001230:Aspergillus / Q000187:drug effects / Q000254:growth & development*; D001231:Aspergillus flavus / Q000187:drug effects / Q000254:growth & development*; D002374:Catalase / Q000378:metabolism; D007700:Kinetics; D008982:Molybdenum / Q000494:pharmacology*; D009565:Nitrate Reductases / Q000378:metabolism; D010544:Peroxidases / Q000378:metabolism; D013045:Species Specificity; D013385:Succinate Dehydrogenase / Q000378:metabolism
chemical_list: D008982:Molybdenum; D010544:Peroxidases; D002374:Catalase; D013385:Succinate Dehydrogenase; D009565:Nitrate Reductases; D000135:Acid Phosphatase; D000154:Aconitate Hydratase