Protein oxidation in plant mitochondria detected as oxidized tryptophan

被引:52
作者
Moller, IM
Kristensen, BK
机构
[1] Royal Vet & Agr Univ, Dept Agr Sci, DK-1871 Frederiksberg C, Denmark
[2] Novo Nordisk AS, Prot Characterizat, DK-2820 Gentofte, Denmark
关键词
mitochondria; mass spectrometry; oxidative stress; protein oxidation; tryptophan; N-formylkynurenine; glycine decarboxylase; complex III; mitochondrial processing peptidase; superoxide dismutase;
D O I
10.1016/j.freeradbiomed.2005.08.036
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The formation of N-formylkynurenine by dioxygenation of tryptophan was detected in peptides from rice leaf and potato tuber mitochondria. Proteins in matrix and membrane fractions were separated by two-dimensional gel electrophoresis and identified using a Q-TOF mass spectrometer. N-Formylkynurenine was detected in 29 peptides representing 17 different proteins. With one exception, the oxidation-sensitive aconitase, all of these proteins were either redox active themselves or subunits in redox-active enzyme complexes. The same site was modified in (i) several adjacent spots containing the P protein of the glycine decarboxylase complex, (ii) two different isoforms of the mitochondrial processing peptidase in complex III, and (iii) the same tryptophan residues in Mn-superoxide dismutase in both rice and potato mitochondria. This indicates that Trp oxidation is a selective process. (c) 2005 Elsevier Inc. All rights reserved.
引用
收藏
页码:430 / 435
页数:6
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