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. Author manuscript; available in PMC: 2016 Dec 1.
Published in final edited form as: Free Radic Biol Med. 2015 Sep 21;89:220–228. doi: 10.1016/j.freeradbiomed.2015.08.003

Table 1.

Biological consequence(s) of Trp oxidation in selected proteins

Protein Oxidant Modification Biological Consequence Refs
Lysozyme Ozone Trps 108 & 111 to NFK No change [57]
Lysozyme Ozone Trp62 to NFK Loss of activity [59]
hSOD1 Bicarbonate radical Intermolecular Trp32 dimerization Protein polymerization/aggregation, potential link to ALS [5,46,63,64]
α-crystallin Singlet oxygen (porphyrins, hypericin, Fenton chemistry), lens aging (unknown oxidant) Trp to NFK, hydroxytryptophans, kynurenine Darkening of lens, potential link to cataractogenesis [53, 67–72]
Apolipoprotein B-100 Hypochlorous acid Trp to kynurenine Modification of LDL into high-uptake form [87]
Apolipoprotein A-1 Hypochlorous acid Trp to hydroxytryptophan and dihydroxytryptophan Modification of HDL that decreases cholesterol efflux capacity [88,89]
D1 Singlet oxygen Trp to NFK Photoinhibition of photosynthesis [91–93]
CP43 Singlet oxygen Trp to NFK Photoinhibition of photosynthesis [91–93]
MopE (Methylococcus capsulatus) Unknown/Endogenous Trp130 to kynurenine, Gain of copper binding function [94]
CorA (Methylomicrobium album BG8) Unknown/Endogenous Trp62 to kynurenine Gain of copper binding function [95]