| Range |
Table - link M^-1×sec^-1
|
| Organism |
Generic |
| Reference |
Davies MJ. Protein oxidation and peroxidation. Biochem J. 2016 Apr 1 473(7):805-25. doi: 10.1042/BJ20151227 p.806 table 2PubMed ID27026395
|
| Primary Source |
[28] Buxton, G.V., Greenstock, C.L., Helman, W.P. and A.B., R. (1988) Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms, and hydroxyl radicals (.OH/.O− ) in aqueous solution. J. Phys. Chem. Ref. Data 17, 513–886 link |
| Comments |
P.805 right column 2nd paragraph: "A wide range of different oxidants (both radical and two-electron) can be generated in vivo, with these arising from multiple external and endogenous processes. These species vary markedly
in their reactivity and the resulting damage is highly variable and complex. Some highly reactive species, such as hydroxyl radicals (HO•, which can arise from exposure to high energy radiation
and metal ion-catalysed decomposition of hydrogen peroxide, H2O2) are capable of oxidizing nearly all biological targets, with second order rate constants near the diffusion limit (i.e. k ∼ 10^9–
10^10 M−1×s−1, Table 2). Due of the abundance of targets in vivo, this results in a microsecond lifetime, and very limited diffusion from its site of generation, so most HO•-induced damage is site specific (e.g. at sites of metal ion binding, or within highly focused
radiation beams)." |
| Entered by |
Uri M |
| ID |
114469 |