Pseudomonas aeruginosa nitrite reductase (or cytochrome oxidase): an overview.
The biochemistry and molecular biology of nitrite reductase, a key enzyme in the dissimilatory denitrification pathway of Ps aeruginosa which reduces nitrite to NO, is reviewed in this paper. The enzyme is a non-covalent homodimer, each subunit containing one heme c and one heme d1. The reaction mechanisms of nitrite and oxygen reduction are discussed in detail, as well as the interaction of the enzyme with its macromolecular substrates, azurin and cytochrome c551. Special attention is paid to new structural information, such as the chemistry of the d1 prosthetic group and the primary sequence of the gene and the protein. Finally, results on the expression both in Ps aeruginosa and in heterologous systems are presented.
Silvestrini
M C
MC
Dipartimento di Scienze Biochimiche, Università di Roma La Sapienza, Italy.
Falcinelli
S
S
Ciabatti
I
I
Cutruzzolà
F
F
Brunori
M
M
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009572:Nitrite Reductases / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics; D013053:Spectrophotometry
D046911:Macromolecular Substances; D009572:Nitrite Reductases; D003576:Electron Transport Complex IV