In the absence of catalytic metals ascorbate does not autoxidize at pH 7: Ascorbate as a test for catalytic metals.

Trace amounts of adventitious transition metals in buffer solutions can serve as catalysts for many oxidative processes. To fully understand what role these metals may play it is necessary that buffer solutions be 'catalytic metal free'. We demonstrate here that ascorbate can be used in a quick and easy test to determine if near-neutral buffer solutions are indeed 'catalytic free'. In buffers which have been rendered free of catalytic metals we have found that ascorbate is quite stable, even at pH 7. The first-order rate constant for the loss of ascorbate in an air-saturated catalytic metal free solution is less than 6 x 10-7 s-1 at pH 7.0. This upper limit appears to be set by the inability to completely eliminate catalytic metal contamination of solutions and glassware. We conclude that in the absence of catalytic metals, ascorbate is stable at pH 7

Spin Trapping: ESR parameters of spin adducts.

Spin trapping has become a valuable tool for the study of free radicals in biology and medicine. The electron spin resonance hyperfine splitting constants of spin adducts of interest in this area are tabulated. The entries also contain a brief comment on the source of the radical trapped

Ascorbate autoxidation in the presence of iron and copper chelates.

Chelates can inhibit the iron- and copper-catalyzed autoxidation of ascorbate at pH 7.0. Diethylenetri-aminepentaacetic acid (DTPA or DETAPAC) and Desferal (deferoximane mesylate) slow the iron-catalyzed oxidation of ascorbate as effectively as reducing the trace levels of contaminating iron in buffers with Chelex resin. DETAPAC, EDTA and HEDTA (N-(2-hydroxyethyl)-ethylenediaminetriacetic acid) are effective at slowing the copper-catalyzed autoxidation of ascorbate while Desferal is ineffective. The ability to inhibit ascorbate autoxidation appears to parallel the rate of the reaction of superoxide with the iron chelate

The kinetics of the reaction of ferritin with superoxide.

Using pulse radiolysis and competition kinetics with cytochrome c, the reaction of superoxide with horse spleen ferritin was investigated. The second-order rate constant is estimated to be 2 ± 1 × 106dm3mol-1s-1

Calcium in lipid peroxidation: Does calcium interact with superoxide?

Using a pulse radiolysis approach to generate and observe superoxide anions (superoxide) in the absence and presence of calcium, we have attempted to verify the recent hypothesis of Babizahyev (Arch. Biochem. Biophys. 266, 446-451, 1988) of a Ca2+-superoxide interaction during lipid peroxidation. We could not observe rapid scavenging of superoxide or complex formation with Ca2+ to account for an inhibitory effect of this cation on lipid peroxidation. Neither could we agree that the stimulatory effect is due to liberation of catalytic ferrous iron from weak complexes by Ca2+. Drawing on reports in the literature, we propose an alternate explanation for the apparent stimulation of lipid peroxidation by low Ca2+ concentrations. In our view, this is not a direct effect, but reflects independently initiated processes of lipid peroxidation and Ca2+ translocation, which interact subsequently in a synergistic manner. The reported inhibition at high Ca2+ concentrations is considered an artifact as it was observed at levels far in excess of those relevant to animal systems (but not necessarily in some plant compartments)