By Lester Packer
This specific, state of the art reference offers a close account of the molecular mechanisms underlying the a number of capabilities of biothiols-emphasizing the organic and scientific implications of interactions among oxidants and biothiols.
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Additional resources for Biothiols in Health and Disease (Antioxidants in Health and Disease Series, 2)
Methods Enzymol. 251:3145. 3. , ed. (1990) Sulfur-Centered Reactive Intermediates in Chemistry and Biology. Plenum Press, New York. 4. -D. (1990) Sulfur-centered free radicals. Methods Enzymol. 186:168180. 5. -D. (1993) Recent aspects of thiyl and perthiyl free radical chemistry. ), pp. 5767, Japan Sci. Soc. Press/CRC Press, Tokyo/Boca Raton, FL. 6. Lal, M. (1994) Radiation induced oxidation of sulphydryl molecules in aqueous solutions. A comprehensive review. Radiat. Phys. Chem. 43:595611. 7. Wardman, P.
GS· then abstracted H from formate/ formic acid over tens/hundreds of microseconds. The stepwise pathway shown in Figure 2 is annotated with the approximate half-lives of each step. It is important that the chromophore-producing final step is not rate-limiting, but that the desired H-abstraction step is. 2. 6 µmol dm-3 GS·, so competing reactions such as Eq. (10) would have a first half-life of ~ 1 ms (10% loss of GS· through Eq. (10) in ~ 120 µs, or over two "divisions" in Fig. 2). It is therefore difficult to exclude completely unwanted, competing reactions such as Eq.
5 mmol dm-3 (48)], only ~2% of thiyl radicals follow the superoxide pathway: most oxidize ascorbate. From this simple calculation, the importance of ascorbate rather than superoxide as a radical "sink" is evident. 4. 5 × 105 dm3 mol-1 s-1. 5 mmol dm-3, superoxide reacts with ascorbate with a half-life of ~ 10 ms. Disproportionation of to form hydrogen peroxide, catalyzed by superoxide dismutase (SOD), would compete with Eq. (32) at this ascorbate concentration if the SOD level was as low as ~ 30 nmol dm-3.