The binding of copper ions to copper-free bovine superoxide dismutase. Applied aspects

✍ Scribed by R. Stevanato; P. Viglino; A. Rigo; D. Cocco; L. Calabrese

• Publisher: Elsevier Science
• Year: 1980
• Tongue: English
• Weight: 218 KB
• Volume: 40
• Category: Article
• ISSN: 0020-1693
• DOI: 10.1016/s0020-1693(00)92154-6

✦ Synopsis

x79 reduction and of reoxidation of the reduced enzyme are affected [6]. Removal of the Type 2 Cu has no effect on the spectroscopic properties of the Type 1 Cu, below pH 7.0, but decreases the enzyme absorbance at 330 nm, usually assigned to the Type 3 Cu, and in the 650-800 nm region. The latter decrease amounts to 250-300 M-' cm-', a rather high value for a 'normal' type of Cu(II) [6]. Similar results were obtained on removal of the Type 2 Cu from ascorbic acid oxidase [7]. The redox potential of the remaining copper ions and the stability of the tree lactase were also affected by removal of the Type 2 cu.

References

1 B. Reinhammar, 'Advances in Inorganic Biochemistry', Eickhorn/MarziIli, eds., 1979, pp. 91-118 and references therein.