Terminal branching of the respiratory electron transport chain in Neisseria meningitidis.
The respiratory components of the envelope membrane preparation of Neisseria meningitidis were investigated. Oxidase activities were demonstrated in this fraction in the presence of succinic acid, reduced nicotinamide adenine dinucleotide, and ascorbate-N,N,N',N'-tetramethyl-p-phenylene-diamine (TMPD). Differences in the kinetics of inhibition by terminal oxidase inhibitors on the three oxidase activities indicated that ascorbate-TMPD oxidation involved only an azide-sensitive oxidase, whereas oxidation of the physiological substrates involved two oxidases, one of which was relatively azide resistant. Spectrophotometric studies revealed that ascorbate-TMPD donated its electrons exclusively to cytochrome o, whereas the physiological substrates were oxidized via both cytochromes o and a. The effects of class II inhibitors on the oxidases suggest terminal branching of the electron transport chain at the cytochrome b level. A model of the respiratory system in N. meningitidis is proposed.
D001205:Ascorbic Acid / Q000378:metabolism; D001386:Azides / Q000494:pharmacology; D003486:Cyanides / Q000494:pharmacology; D003580:Cytochromes / Q000378:metabolism*; D004579:Electron Transport; D006898:Hydroxylamines / Q000494:pharmacology; D009097:Multienzyme Complexes / Q000378:metabolism*; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D009345:Neisseria meningitidis / Q000378:metabolism*; D010101:Oxygen Consumption; D013385:Succinate Dehydrogenase / Q000378:metabolism*; D013772:Tetramethylphenylenediamine / Q000378:metabolism
D001386:Azides; D003486:Cyanides; D003580:Cytochromes; D006898:Hydroxylamines; D009097:Multienzyme Complexes; D013385:Succinate Dehydrogenase; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases; D013772:Tetramethylphenylenediamine; D001205:Ascorbic Acid