期刊
ANALYTICAL CHEMISTRY
卷 88, 期 24, 页码 12060-12065出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.6b02502
关键词
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资金
- China State Key Basic Research Program Grant [2013CB911203]
- China State Key Research Grant [2016YFA0501402]
- National Natural Science Foundation of China [21675152, 21305139, 21573223]
- Youth Innovation Promotion Association of CAS [2014164]
- Strategic Priority Research Program of CAS [XDB17030100]
- Grants-in-Aid for Scientific Research [24000018] Funding Source: KAKEN
Positively charged lysines are crucial to maintaining the native structures of proteins and protein complexes by forming hydrogen bonds and electrostatic interactions with their proximal amino acid residues. However, it is still a challenge to develop an efficient method for probing the active proximal microenvironments of lysines without changing their biochemical/physical properties. Herein, we developed an active covalent labeling strategy combined with mass spectrometry to systematically probe the lysine proximal microenvironments within membrane protein complexes (similar to 700 kDa) with high throughput. Our labeling strategy has the advantages of high labeling efficiency and stability, preservation of the active charge states, as well as biological activity of the labeled proteins. In total, 121 lysines with different labeling levels were obtained for the photosystem II complexes from cyanobacteria, red algae, and spinach and provided important insights for understanding the conserved and nonconserved local structures of PSII complexes among evolutionarily divergent species that perform photosynthesis.
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