Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation
A major question in redox signaling is how H2O2 oxidizes target protein thiols in the presence of glutathione peroxidases and peroxiredoxins. We reveal signaling by H2O2 via its enzymatic conversion to an alkyl hydroperoxide that stereo-specifically escapes peroxidases and oxidizes target proteins.
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Nature Portfolio
2021
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oai:doaj.org-article:16b1acb3e2684793a89d03d6d3dc92b42021-11-21T12:34:06ZHydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation10.1038/s41467-021-26991-52041-1723https://doaj.org/article/16b1acb3e2684793a89d03d6d3dc92b42021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26991-5https://doaj.org/toc/2041-1723A major question in redox signaling is how H2O2 oxidizes target protein thiols in the presence of glutathione peroxidases and peroxiredoxins. We reveal signaling by H2O2 via its enzymatic conversion to an alkyl hydroperoxide that stereo-specifically escapes peroxidases and oxidizes target proteins.Raphael F. QueirozChristopher P. StanleyKathryn WolhuterStephanie M. Y. KongRagul RajivanNaomi McKinnonGiang T. H. NguyenAntonella RoveriSebastian GuttzeitPhilip EatonWilliam A. DonaldFulvio UrsiniChristine C. WinterbournAnita AyerRoland StockerNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-17 (2021) |
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Science Q Raphael F. Queiroz Christopher P. Stanley Kathryn Wolhuter Stephanie M. Y. Kong Ragul Rajivan Naomi McKinnon Giang T. H. Nguyen Antonella Roveri Sebastian Guttzeit Philip Eaton William A. Donald Fulvio Ursini Christine C. Winterbourn Anita Ayer Roland Stocker Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation |
description |
A major question in redox signaling is how H2O2 oxidizes target protein thiols in the presence of glutathione peroxidases and peroxiredoxins. We reveal signaling by H2O2 via its enzymatic conversion to an alkyl hydroperoxide that stereo-specifically escapes peroxidases and oxidizes target proteins. |
format |
article |
author |
Raphael F. Queiroz Christopher P. Stanley Kathryn Wolhuter Stephanie M. Y. Kong Ragul Rajivan Naomi McKinnon Giang T. H. Nguyen Antonella Roveri Sebastian Guttzeit Philip Eaton William A. Donald Fulvio Ursini Christine C. Winterbourn Anita Ayer Roland Stocker |
author_facet |
Raphael F. Queiroz Christopher P. Stanley Kathryn Wolhuter Stephanie M. Y. Kong Ragul Rajivan Naomi McKinnon Giang T. H. Nguyen Antonella Roveri Sebastian Guttzeit Philip Eaton William A. Donald Fulvio Ursini Christine C. Winterbourn Anita Ayer Roland Stocker |
author_sort |
Raphael F. Queiroz |
title |
Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation |
title_short |
Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation |
title_full |
Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation |
title_fullStr |
Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation |
title_full_unstemmed |
Hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation |
title_sort |
hydrogen peroxide signaling via its transformation to a stereospecific alkyl hydroperoxide that escapes reductive inactivation |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/16b1acb3e2684793a89d03d6d3dc92b4 |
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