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Protein Science, Vol 7, Issue 11 2391-2397, Copyright © 1998 by Cold Spring Harbor Laboratory Press

ARTICLE

Identification of tryptophan oxidation products in bovine {alpha}-crystallin

E. L. FINLEY, J. DILLON, R. K. CROUCH and K. L. SCHEY
Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, 171 Ashley Avenue, Charleston, South Carolina 29425

Oxidation is known to affect the structure, activity, and rate of degradation of proteins, and is believed to contribute to a variety of pathological conditions. Metal-catalyzed oxidation (MCO) is a primary oxidizing system in many cell types. In this study, the oxidative effects of a MCO system (the Fenton reaction) on the structure of the tryptophan residues of {alpha}-crystallin were determined. Tandem mass spectrometry (MS/MS) was utilized to identify specific tryptophan and methionine oxidation products in the bovine {alpha}-crystallin sequence. After oxidative exposure, {alpha}-crystallin was digested with trypsin, and the resulting peptides were fractionated by reverse-phase HPLC. Structural analysis by mass spectrometry revealed that tryptophan 9 of {alpha}A- and tryptophan 60 of {alpha}B-crystallin were each converted into hydroxytryptophans (HTRP), N-formylkynurenine (NFK), and kynurenine (KYN). However, only HTRP and KYN formation were detected at residue 9 of {alpha}B-crystallin. Oxidation of methionine 1 of {alpha}A- and methionine 1 and 68 of {alpha}B-crystallin was also detected. The products NFK and KYN are of particular importance in the lens, as they themselves are photosensitizers that can generate reactive oxygen species (ROS) upon UV light absorption. The unambiguous identification of HTRP, NFK, and KYN in intact {alpha}-crystallin represents the first structural proof of the formation of these products in an intact protein, and provides a basis for detailed structural analysis of oxidized proteins generated in numerous pathological conditions.
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