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.
NO production by Pseudomonas aeruginosa cd1 nitrite reductase / Cutruzzola', Francesca; Rinaldo, Serena; Centola, F; Brunori, Maurizio. - In: IUBMB LIFE. - ISSN 1521-6543. - 55:10-11(2003), pp. 617-621. [10.1080/15216540310001628672]
NO production by Pseudomonas aeruginosa cd1 nitrite reductase.
CUTRUZZOLA', Francesca;RINALDO, Serena;BRUNORI, Maurizio
2003
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
