Conformational aspects of superoxide-dismutase-active copper chelates and catechols
β Scribed by Ulrich Weser; Lutz M. Schubotz
- Publisher
- Elsevier Science
- Year
- 1978
- Weight
- 904 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0006-3061
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β¦ Synopsis
The pos$ile structxai basis of the specific i&Story action of cuprein on the autoxidation of catfqchola+ne wasexamined. The chjro&al properties -_ of the native enzyme were compared with both tlk denatukd tid the apo-' protein and-i& stiperoxide-disnutasease-active Cu(T$r)p. A&rt froth the reduc-' tion of cuprein copper to Cu(I);marked and chaiact&stic k-es @ ihe -1 circuIar dichroism (CD) spectrum from 260-400 nm jn the-presence bf tidrena-. .I. line and oxygen were seen, suggesti& the. foq&ion of .a ternary compkx.
_.
This conformatikial change proved dep&ae& od the coke&&o~ oi Oxygen, adrenaline, Bnd -cuprein copper and was: not-keen..when the apo&oteti or &heat-denatured enzyme was used.
π SIMILAR VOLUMES
The copper(II) complexes of the Schiff base salicylaldehyde semicarbazone (SALSC) have been prepared and structurally characterized. The compound possesses a distorted square planar geometry where the metal atom lies slightly below the ligand donor atom plane and exhibits a longer Cu-Cl bond distanc