Glutaredoxin catalysis requires two distinct glutathione interaction sites

Glutaredoxins have important roles in redox processes. Here the authors show that the enzymatic activity of glutaredoxins requires two distinct glutathione interactions sites, one recognizing the glutathione disulfide substrate and one activating glutathione as a reducing agent.

Bibliographic Details
Main Authors: Patricia Begas, Linda Liedgens, Anna Moseler, Andreas J. Meyer, Marcel Deponte
Format: Article
Language:English
Published: Nature Publishing Group 2017-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms14835
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spelling doaj-740639bdf8af4d88af583ed4dd6926cd2021-05-11T07:51:27ZengNature Publishing GroupNature Communications2041-17232017-04-018111310.1038/ncomms14835Glutaredoxin catalysis requires two distinct glutathione interaction sitesPatricia Begas0Linda Liedgens1Anna Moseler2Andreas J. Meyer3Marcel Deponte4Department of Parasitology, Ruprecht-Karls UniversityDepartment of Parasitology, Ruprecht-Karls UniversityInstitute of Crop Science and Resource Conservation (INRES)-Chemical Signalling, University of BonnInstitute of Crop Science and Resource Conservation (INRES)-Chemical Signalling, University of BonnDepartment of Parasitology, Ruprecht-Karls UniversityGlutaredoxins have important roles in redox processes. Here the authors show that the enzymatic activity of glutaredoxins requires two distinct glutathione interactions sites, one recognizing the glutathione disulfide substrate and one activating glutathione as a reducing agent.https://doi.org/10.1038/ncomms14835
collection DOAJ
language English
format Article
sources DOAJ
author Patricia Begas
Linda Liedgens
Anna Moseler
Andreas J. Meyer
Marcel Deponte
spellingShingle Patricia Begas
Linda Liedgens
Anna Moseler
Andreas J. Meyer
Marcel Deponte
Glutaredoxin catalysis requires two distinct glutathione interaction sites
Nature Communications
author_facet Patricia Begas
Linda Liedgens
Anna Moseler
Andreas J. Meyer
Marcel Deponte
author_sort Patricia Begas
title Glutaredoxin catalysis requires two distinct glutathione interaction sites
title_short Glutaredoxin catalysis requires two distinct glutathione interaction sites
title_full Glutaredoxin catalysis requires two distinct glutathione interaction sites
title_fullStr Glutaredoxin catalysis requires two distinct glutathione interaction sites
title_full_unstemmed Glutaredoxin catalysis requires two distinct glutathione interaction sites
title_sort glutaredoxin catalysis requires two distinct glutathione interaction sites
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-04-01
description Glutaredoxins have important roles in redox processes. Here the authors show that the enzymatic activity of glutaredoxins requires two distinct glutathione interactions sites, one recognizing the glutathione disulfide substrate and one activating glutathione as a reducing agent.
url https://doi.org/10.1038/ncomms14835
work_keys_str_mv AT patriciabegas glutaredoxincatalysisrequirestwodistinctglutathioneinteractionsites
AT lindaliedgens glutaredoxincatalysisrequirestwodistinctglutathioneinteractionsites
AT annamoseler glutaredoxincatalysisrequirestwodistinctglutathioneinteractionsites
AT andreasjmeyer glutaredoxincatalysisrequirestwodistinctglutathioneinteractionsites
AT marceldeponte glutaredoxincatalysisrequirestwodistinctglutathioneinteractionsites
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