Localization of tetramethylphenylenediamine-oxidase in the outer cell wall layer of Neisseria meningitidis.
A highly active tetramethylphenylenediamine-oxidase has been found in association with the cell wall blebs, evaginations of the outer wall membrane, of Neisseria meningitidis. Isolated wall blebs consumed oxygen in the presence of ascorbate-tetramethylphenylenediamine but not in the presence of succinate, whereas cell envelope preparations are active in both substrates. The ratio of succinate dehydrogenase/tetramethylphenylenediamine-oxidase activities in preparations of envelopes was approximately 100 times that in isolated wall blebs, indicating that the outer membrane preparations were highly purified.
D002458:Cell Fractionation; D002473:Cell Wall / Q000201:enzymology; D003486:Cyanides / Q000494:pharmacology; D009345:Neisseria meningitidis / Q000201:enzymology* / Q000378:metabolism / Q000648:ultrastructure; D010088:Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D010101:Oxygen Consumption; D013385:Succinate Dehydrogenase / Q000378:metabolism; D013772:Tetramethylphenylenediamine
D003486:Cyanides; D010088:Oxidoreductases; D013385:Succinate Dehydrogenase; D013772:Tetramethylphenylenediamine