Localization of tetramethylphenylenediamine-oxidase in the outer cell wall layer of Neisseria meningitidis.

Abstract

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.

• Authors: I W Devoe, J E Golchrist
• Journal: Journal of bacteriology (J Bacteriol) Vol. 128 Issue 1 Pg. 144-8 (Oct 1976) ISSN: 0021-9193 [Print] United States
• PMID: 824266 (Publication Type: Journal Article)

Chemical References

• Cyanides
• Oxidoreductases
• Succinate Dehydrogenase
• Tetramethylphenylenediamine

Topics

• Cell Fractionation
• Cell Wall (enzymology)
• Cyanides (pharmacology)
• Neisseria meningitidis (enzymology, metabolism, ultrastructure)
• Oxidoreductases (isolation & purification, metabolism)
• Oxygen Consumption
• Succinate Dehydrogenase (metabolism)
• Tetramethylphenylenediamine