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 d(1). 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 c(551). Special attention is paid to new structural information, such as the chemistry of the d(1) 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.
Pseudomonas aeruginosa nitrite reductase (or cytochrome oxidase): an overview / Silvestrini, Mc; Falcinelli, S; Ciabatti, I; Cutruzzola', Francesca; Brunori, Maurizio. - In: BIOCHIMIE. - ISSN 0300-9084. - 76:7(1994), pp. 641-654. [10.1016/0300-9084(94)90141-4]
Pseudomonas aeruginosa nitrite reductase (or cytochrome oxidase): an overview.
CUTRUZZOLA', Francesca;BRUNORI, Maurizio
1994
Abstract
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 d(1). 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 c(551). Special attention is paid to new structural information, such as the chemistry of the d(1) 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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
