Differential binding of anions to the active site of Cu,Zn superoxide dismutase. A study of the Co,Zn enzyme derivative.

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.

journal_name

J Inorg Biochem

authors

Desideri A,Paci M,Capo C,Calabrese L,Rotilio G

doi

10.1016/0162-0134(88)80006-0

subject

Has Abstract

pub_date

1988-08-01 00:00:00

pages

277-83

issue

4

eissn

0162-0134

issn

1873-3344

pii

0162-0134(88)80006-0

journal_volume

33

pub_type

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