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Open Access Green as soon as Postprint is submitted to ZB.
An expanded function for superoxide dismutase.
Free Radic. Res. 12, 411-417 (1991)
αHydroxyalkylperoxyl radicals were generated from the primary and secondary alcohols methanol, ethanol and 2-propanol in N2O/O2-saturated aqueous solutions by pulse radiolysis. These radicals reduced a ferric iron porphyrin complex, tetrakis-(4-N-methylpyridyl)porphine, with diffusiontontrolled rate constants. The extreme sensitivity of the shift of the Soret absorption band in this reaction was used to determine, by competition kinetics, the reactivity of the peroxyl radicals with different proteins. Only native Cu, Zn-superoxide dismutase and metallothionein showed competitive behavior, with SOD exhibiting rate constants close to the dismutation rate for O2- Metallothionein was slower by a factor of 30 with hydroxymethylperoxyl radicals. We propose, that SOD has unique properties of the protein surface in addition to the prosthetic copper site, having possibly evolved as a 'general-purpose radical-scavenging protein'.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Alcohol Peroxyl Radicals ; Competition Kinetics ; Iron Porphyrin Complex ; Pulse Radiolysis ; Rate Constants
ISSN (print) / ISBN
1071-5762
e-ISSN
1029-2470
Journal
Free Radical Research
Quellenangaben
Volume: 12,
Issue: 1,
Pages: 411-417
Publisher
Taylor & Francis
Reviewing status
Peer reviewed
Institute(s)
Abteilung für Strahlenbiologie und Biophysik