Chiral methionine oxidation reagents reveal stereospecific proteome modifications

2026 · doi:10.64898/2026.03.24.713977
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⚙ AI-generated summary by claude@2026-07, 2026-07-14 ⓘ

Enantiomeric oxaziridine reagents identify stereospecific methionine oxidation sites in proteomes that are reversed by methionine sulfoxide reductases, revealing chiral regulation of protein function and oxidative stress responses.

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⚙ AI-generated deep summary by claude@2026-07, 2026-07-14 · read from full text ⓘ

The study developed enantiomeric oxaziridine reagents to stereospecifically label and identify pro-(S) versus pro-(R) methionine oxidation sites across proteomes, with oxidation signals removed by methionine sulfoxide reductase A or B, respectively. In cell and murine oxidative-stress models, the authors found that selective (R)-methionine sulfoxide formation at M69 of biphenyl hydrolase-like protein inhibited hydrolase activity and increased proteome N-homocysteinylation, indicating that chiral methionine redox regulation can allosterically control protein function. A key caveat is that the work relies on reagent-based chemical labeling and specific reductase activities to assign the oxidation stereochemistry and its downstream effects. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

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Abstract

Life is predicated on chirality, a molecular asymmetry akin to the left and right versions of human hands. Here we show that privileged protein residues are predisposed for chiral regulation. We developed enantiomeric oxaziridine reagents that systematically identify pro-( S ) and pro-( R ) methionine oxidation sites across proteomes that can be erased by stereospecific methionine sulfoxide reductase enzymes A and B, respectively. These probes reveal that chiral regulation of methionine oxidation-reduction processes can allosterically regulate protein function, as shown in cell and murine models of oxidative stress where selective ( R )-methionine sulfoxide formation on M69 of biphenyl hydrolase-like protein leads to hydrolase inhibition and amplification of proteome N -homocysteinylation modifications. This work introduces a platform for characterizing sites of asymmetric methionine oxidation and the functional consequences concomitant with an individual chiral single-atom modification.
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Abstract Life is predicated on chirality, a molecular asymmetry akin to the left and right versions of human hands. Here we show that privileged protein residues are predisposed for chiral regulation. We developed enantiomeric oxaziridine reagents that systematically identify pro-(S) and pro-(R) methionine oxidation sites across proteomes that can be erased by stereospecific methionine sulfoxide reductase enzymes A and B, respectively. These probes reveal that chiral regulation of methionine oxidation-reduction processes can allosterically regulate protein function, as shown in cell and murine models of oxidative stress where selective (R)-methionine sulfoxide formation on M69 of biphenyl hydrolase-like protein leads to hydrolase inhibition and amplification of proteome N-homocysteinylation modifications. This work introduces a platform for characterizing sites of asymmetric methionine oxidation and the functional consequences concomitant with an individual chiral single-atom modification. Competing Interest Statement The authors have declared no competing interest.

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