Characterization of bacterial cytochrome cd(1)-nitrite reductase as one enzyme responsible for catalysis of nitrosation of secondary amines.
Bacterial formation of carcinogenic N-nitroso compounds may play a role in the etiology of human cancer. Biochemical and immunological studies in denitrifying bacteria (Pseudomonas aeruginosa) strongly support the identification of cytochrome cd(1)-nitrite reductase as the enzyme responsible for the catalysis of nitrosation through the production of nitric oxide or NO(+)-like species. Interestingly, electron paramagnetic resonance studies have shown that large quantities of nitric oxide or NO(+)-species were also produced by non-denitrifying enterobacteria (Escherichia coli, Proteus morganii).
Calmels
S
S
International Agency for Research on Cancer, Lyon, France.
Ohshima
H
H
Henry
Y
Y
Bartsch
H
H
D000906:Antibodies / Q000494:pharmacology; D003574:Cytochrome c Group; D003580:Cytochromes / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D009569:Nitric Oxide / Q000032:analysis*; D009572:Nitrite Reductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D015538:Nitrosation; D011511:Proteus / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000201:enzymology; D013056:Spectrophotometry, Ultraviolet
D000906:Antibodies; D003574:Cytochrome c Group; D003580:Cytochromes; D009569:Nitric Oxide; C019315:cytochrome cd1; D009572:Nitrite Reductases