The reaction of N3- with Co,Zn superoxide dismutase, a good analogue of the native Cu,Zn enzyme, was studied in the presence and absence of phosphate, which is known to perturb the spectroscopic properties of the cobalt chromophore in the Co,Zn enzyme. EPR, NMR, and optical titrations demonstrated the formation of different adducts for N3- depending on the presence of phosphate, at variance with results previously obtained with CN- [3]. This evidence indicates that the mechanism of anion binding to Cu,Zn superoxide dismutase cannot be described on the basis of data obtained with a single type of anions.
Desideri, A., Paci, M., Capo, C., Calabrese, L., Rotilio, G. (1988). Differential binding of anions to the active site of Cu,Zn superoxide dismutase. A study of the Co,Zn enzyme derivative. JOURNAL OF INORGANIC BIOCHEMISTRY, 33(4), 277-283 [10.1016/0162-0134(88)80006-0].
Differential binding of anions to the active site of Cu,Zn superoxide dismutase. A study of the Co,Zn enzyme derivative
DESIDERI, ALESSANDRO;PACI, MAURIZIO;CALABRESE, LEONARDO;ROTILIO, GIUSEPPE
1988-08-01
Abstract
The reaction of N3- with Co,Zn superoxide dismutase, a good analogue of the native Cu,Zn enzyme, was studied in the presence and absence of phosphate, which is known to perturb the spectroscopic properties of the cobalt chromophore in the Co,Zn enzyme. EPR, NMR, and optical titrations demonstrated the formation of different adducts for N3- depending on the presence of phosphate, at variance with results previously obtained with CN- [3]. This evidence indicates that the mechanism of anion binding to Cu,Zn superoxide dismutase cannot be described on the basis of data obtained with a single type of anions.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
