ArticleProtein science : a publication of the Protein Society2019
Crystallographic identification of spontaneous oxidation intermediates and products of protein sulfhydryl groups.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 21 citations in OpenAlex.
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- Antigenic assessment for the β2-glycoprotein I/Platelet factor 4 complex in thrombotic patients with antiphospholipid syndrome.Frontiers in immunology · 2025Article
- Structural Features ofToxins · 2022Article
- Widespread occurrence of covalent lysine-cysteine redox switches in proteins.Nature chemical biology · 2022Article
- Recognizing lysine-cysteine crosslinks in proteins.Protein science : a publication of the Protein Society · 2021Article
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- The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021Review
- Crystal structure of the C-terminal domain of DENR.Computational and structural biotechnology journal · 2020Article
- Comment on Wang's paper on the covalent Cys-X-Lys bridges.Protein science : a publication of the Protein Society · 2019Article
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Abstract
In the absence of protective reducing agents, Cys residues in purified proteins can be oxidized spontaneously by oxygen in the air, as frequently observed in protein crystal structures. However, the formation of an O-bridge via dehydration mechanism between a peroxidized Cys side chain and a primary amine of Lys side chain in proteins has not yet been reported. When an electron density feature was observed for an extra group or an extra atom between side chains of Cys-245 and Lys-158 in the crystal structure of histidinol phosphate phosphatase, mass spectrometric analysis was carried out for its chemical identification. That analysis led to a conclusion that this extra density corresponded to a methylene group. It was then proposed that these two residues were able to absorb CO
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