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. 2017 Mar 6;114(11):2988–2993. doi: 10.1073/pnas.1618922114

Table S1.

Time course of oxidative modifications of D1 and D2 proteins

Protein 0 min 15 min 30 min
D1 316T +go* 316T+go 1M+to
317W+do,go 317W+do, go, kyn 7R+ca
319D+go 328M+go 130E+go
328M+go 331M+go 131W+go
331M+go 332H+go 315N+go
333E+go 316T+go
317W+do, go, kyn
319D+go
329E+go
331M+go
332H+go
333E+go
D2 18M+go 18M+go 18M+go
246M+go 246M,+go 242E+de
247V+go 247V+go 244Y+go
329M+go 328W+go, 245S+go
329M+go, do 333D+go 246M+go
334Q+go 247V+go
336H+hro 328W+do, kyn 329M+do, go, to
333D+gam
341F+go
342P+go
343E+ca, de
344E+de, go
345V+go
*

Oxidative modifications key: do, double oxidation, +31.99 Da; gam, Glu/Asp decarboxylation, −30.01 Da; go, general oxidation, +15.99 Da; hro, histidine ring opening, −10.03 Da; kyn, kynurenine formation, +3.99 Da; to, triple oxidation, +47.98 Da. In some instances, more than one type of modification was observed for a particular amino acid residue on different identified peptides, these are separated by commas. It should be noted that whereas a total of 12 different types of oxidative modifications were incorporated into the MassMatrix searches, only these 6 types were actually observed in this study.