ArticleThe Journal of biological chemistry2022
Protein folding stabilities are a major determinant of oxidation rates for buried methionine residues.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 35 citations in OpenAlex.
- Nutritional Evaluation and Protein Quality Assessment of Green Peas (Pisum sativum L.) Treated with Different Cooking Methods.Plant foods for human nutrition (Dordrecht, Netherlands) · 2026Article
- Structural proteomics reveals that misfolded nascent proteins expose buried lysines for ubiquitination and rapid proteasomal degradation.Cell reports · 2026Article
- Data-Independent Acquisition (DIA) Strategy for Measuring Protein Stability Using Stability of Proteins from Rates of Oxidation (SPROX).Journal of the American Society for Mass Spectrometry · 2026Article
- Photooxidative molecular damage under blue light.Experimental & molecular medicine · 2026Review
- Methionine Oxidation Footprinting in Intact Proteins (MOFIP) Using Top-Down Proteomics.Proteomics · 2025Article
- Antioxidant evolution of fibrinogen: a crucial role of methionines.Biophysical reviews · 2025Review
- Quantitative readout of methionine residue solvent accessibility in E. coli cells using radiolytic hydroxyl radical labeling and mass spectrometry.Biochemical and biophysical research communications · 2025Article
- Thiol-based redox sensing regulates the yellow pigment and antioxidant accumulation and improves the nutritional quality of wheat grains (Frontiers in plant science · 2025Article
- Hidden route of protein damage through oxygen-confined photooxidation.Nature communications · 2024Article
- Formylation facilitates the reduction of oxidized initiator methionines.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Methionine Alkylation as an Approach to Quantify Methionine Oxidation Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Folding stabilities of ribosome-bound nascent polypeptides probed by mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Antioxidant role of methionine-containing intra- and extracellular proteins.Biophysical reviews · 2023Review
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- CJournal of proteome research · 2023Article
- Interplay of carbon dioxide and peroxide metabolism in mammalian cells.The Journal of biological chemistry · 2022Review
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7 authors at 1 institution in 1 country.
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Abstract
The oxidation of protein-bound methionines to form methionine sulfoxides has a broad range of biological ramifications, making it important to delineate factors that influence methionine oxidation rates within a given protein. This is especially important for biopharmaceuticals, where oxidation can lead to deactivation and degradation. Previously, neighboring residue effects and solvent accessibility have been shown to impact the susceptibility of methionine residues to oxidation. In this study, we provide proteome-wide evidence that oxidation rates of buried methionine residues are also strongly influenced by the thermodynamic folding stability of proteins. We surveyed the Escherichia coli proteome using several proteomic methodologies and globally measured oxidation rates of methionine residues in the presence and absence of tertiary structure, as well as the folding stabilities of methionine-containing domains. These data indicated that buried methionines have a wide range of protection factors against oxidation that correlate strongly with folding stabilities. Consistent with this, we show that in comparison to E. coli, the proteome of the thermophile Thermus thermophilus is significantly more stable and thus more resistant to methionine oxidation. To demonstrate the utility of this correlation, we used native methionine oxidation rates to survey the folding stabilities of E. coli and T. thermophilus proteomes at various temperatures and propose a model that relates the temperature dependence of the folding stabilities of these two species to their optimal growth temperatures. Overall, these results indicate that oxidation rates of buried methionines from the native state of proteins can be used as a metric of folding stability.
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