Proteolitic digestion of nitrite reductase from Pseudomonas aeruginosa allows to obtain and purify a domain containing only the d(1) heme and constituted by two noncovalently bound peptides. This d(1) domain catalyzes oxygen consumption, and binds carbon monoxide with a kinetic constant slightly higher than the parental dimeric holoenzyme. The capacity to oxidize the physiological substrate, cytochrome c(551), is lost, even when the proteolytic c heme domain is added to this reaction mixture. This finding suggests that the two domains do not have a significant affinity for each other, and are kept together only by being part of the same polypeptide.
Isolation and characterization of the d(1) domain of Pseudomonas aeruginosa nitrite reductase / Silvestrini, Mc; Cutruzzola', Francesca; Schinina', Maria Eugenia; Maras, Bruno; Rolli, G; Brunori, Maurizio. - In: JOURNAL OF INORGANIC BIOCHEMISTRY. - ISSN 0162-0134. - 62:2(1996), pp. 77-87. [10.1016/0162-0134(95)00090-9]
Isolation and characterization of the d(1) domain of Pseudomonas aeruginosa nitrite reductase
CUTRUZZOLA', Francesca;SCHININA', Maria Eugenia;MARAS, Bruno;BRUNORI, Maurizio
1996
Abstract
Proteolitic digestion of nitrite reductase from Pseudomonas aeruginosa allows to obtain and purify a domain containing only the d(1) heme and constituted by two noncovalently bound peptides. This d(1) domain catalyzes oxygen consumption, and binds carbon monoxide with a kinetic constant slightly higher than the parental dimeric holoenzyme. The capacity to oxidize the physiological substrate, cytochrome c(551), is lost, even when the proteolytic c heme domain is added to this reaction mixture. This finding suggests that the two domains do not have a significant affinity for each other, and are kept together only by being part of the same polypeptide.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
