Abstract
The ability of Neisseria meningitidis to utilize both oxygen and nitrogen oxides as respiratory substrates allows it to thrive in the diverse environment of the human host. Genome analysis highlighted genes encoding a cbb(3) cytochrome oxidase, the aniA nitrite reductase gene and the norB nitric oxide reductase gene. In the present study, we used myxothiazol as an inhibitor of the bc(1) complex in intact cells and demonstrated that electron flow to nitrite reductase and the cytochrome oxidase, but not NO reductase, passes via the cytochrome bc(1) complex. UV-visible spectrophotometry of intact cells demonstrated that oxygen oxidizes c-type and b-type cytochromes. oxidation of cytochromes by nitrite was only seen in microaerobically precultured whole cells, and the predominant oxidizable cytochromes were b-type. These are likely to be associated with the oxidation of a b-haem-containing nitric oxide reductase. Nitrite inhibits the oxidation of cytochromes by oxygen in a nitrite reductase-independent manner, indicating that nitrite may inhibit oxidase activity directly, as well as via the intermediate of denitrification, nitric oxide.
| Original language | English |
|---|---|
| Pages (from-to) | 139-142 |
| Number of pages | 4 |
| Journal | Biochemical Society transactions |
| Volume | 34 |
| Publication status | Published - Feb 2006 |
Keywords
- branched respiratory chain
- cupredoxin
- cytochrome
- denitrification
- myxothiazol
- Neisseria meningitidis
- DENITRIFICATION
- NITRITE