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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Autores principales: 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
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/16b1acb3e2684793a89d03d6d3dc92b4
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spelling 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)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle 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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