NO production by Pseudomonas aeruginosa cd1 nitrite reductase.
The structural and catalytic properties of Pseudomonas aeruginosa cd1 nitrite reductase, a key enzyme in bacterial denitrification, are reviewed in this paper. The mechanism of reduction of nitrite to NO is discussed in detail with special attention to the structural interpretation of function. The ability to stabilize negatively charged molecules, such as the substrate (nitrite) and other ligands (hydroxide and cyanide), is a key feature of catalysis in cd1NIRs. The positive potential in the active site is largely due to the presence of the two conserved distal histidines, which are involved in both substrate binding and product release.
Cutruzzolà
Francesca
F
Dipartimento di Scienze Biochimiche, Universita di Roma La Sapienza, 00185 Rome, Italy. francesca.cutruzzola@uniroma1.it
Rinaldo
Serena
S
Centola
Fabio
F
Brunori
Maurizio
M
D003580:Cytochromes; D019281:Dimerization; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D009569:Nitric Oxide / Q000378:metabolism*; D009572:Nitrite Reductases / Q000737:chemistry* / Q000378:metabolism; D009573:Nitrites / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D003580:Cytochromes; D008024:Ligands; D009573:Nitrites; D009569:Nitric Oxide; D009572:Nitrite Reductases; C028123:nitrite reductase (NO-forming); D003576:Electron Transport Complex IV