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NO Production by Pseudomonas aeruginosa cd1 Nitrite Reductase
Author(s) -
Cutruzzolà Francesca,
Rinaldo Serena,
Centola Fabio,
Brunori Maurizio
Publication year - 2003
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540310001628672
Subject(s) - nitrite reductase , nitrite , pseudomonas aeruginosa , chemistry , cyanide , hydroxide , substrate (aquarium) , reductase , catalysis , biochemistry , active site , enzyme , bacteria , nitrate reductase , inorganic chemistry , nitrate , biology , organic chemistry , ecology , genetics
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. IUBMB Life, 55: 617‐621, 2003