Selected apparent second order rate constants for reaction of HOCl with amino acid side chains, backbone amides and models of these structures

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 4PubMed ID27026395
Primary Source [278] Storkey C., Davies M.J., Pattison D.I. (2014) Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach. Free Radic. Biol. Med. 73:60–66 doi:10.1016/j.freeradbiomed.2014.04.024 [281] Pattison D.I., Davies M.J. (2001) Absolute rate constants for the reaction of hypochlorous acid with protein side-chains and peptide bonds. Chem. Res. Toxicol. 14:1453–1464 doi:10.1021/tx0155451 [282] Pattison D.I., Davies M.J. (2006) Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining insight into human inflammatory disease. Curr. Med. Chem. 13:3271–3290 doi:10.2174/092986706778773095PubMed ID24794410, 11599938, 17168851
Comments P.806 left column bottom paragraph: "There can also be enormous variations in the rate constants for a single oxidant with different biological targets. Thus in contrast with HO• where there are only relatively minor variations in k between targets (see above), other oxidants such as hypochlorous acid (HOCl, a major oxidant generated at sites of inflammation by neutrophils and monocytes) react with the various side chains present on proteins with k values that vary by ∼10^11 (Table 4)."
Entered by Uri M
ID 114481