Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase

Due to their transient nature, enzyme-substrate complexes are difficult to characterize structurally. Here, the authors capture the reactive reduced form of xenobiotic reductase A bound to its substrate and show that the oxidation state of the flavin cofactor affects the interaction of the substrate...

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Autores principales: Tobias Werther, Stefan Wahlefeld, Johannes Salewski, Uwe Kuhlmann, Ingo Zebger, Peter Hildebrandt, Holger Dobbek
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/6e5f0d2118e441349f25a2bde1c8e4d9
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spelling oai:doaj.org-article:6e5f0d2118e441349f25a2bde1c8e4d92021-12-02T14:41:07ZRedox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase10.1038/ncomms160842041-1723https://doaj.org/article/6e5f0d2118e441349f25a2bde1c8e4d92017-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms16084https://doaj.org/toc/2041-1723Due to their transient nature, enzyme-substrate complexes are difficult to characterize structurally. Here, the authors capture the reactive reduced form of xenobiotic reductase A bound to its substrate and show that the oxidation state of the flavin cofactor affects the interaction of the substrate with the enzyme.Tobias WertherStefan WahlefeldJohannes SalewskiUwe KuhlmannIngo ZebgerPeter HildebrandtHolger DobbekNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-8 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Tobias Werther
Stefan Wahlefeld
Johannes Salewski
Uwe Kuhlmann
Ingo Zebger
Peter Hildebrandt
Holger Dobbek
Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
description Due to their transient nature, enzyme-substrate complexes are difficult to characterize structurally. Here, the authors capture the reactive reduced form of xenobiotic reductase A bound to its substrate and show that the oxidation state of the flavin cofactor affects the interaction of the substrate with the enzyme.
format article
author Tobias Werther
Stefan Wahlefeld
Johannes Salewski
Uwe Kuhlmann
Ingo Zebger
Peter Hildebrandt
Holger Dobbek
author_facet Tobias Werther
Stefan Wahlefeld
Johannes Salewski
Uwe Kuhlmann
Ingo Zebger
Peter Hildebrandt
Holger Dobbek
author_sort Tobias Werther
title Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
title_short Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
title_full Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
title_fullStr Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
title_full_unstemmed Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
title_sort redox-dependent substrate-cofactor interactions in the michaelis-complex of a flavin-dependent oxidoreductase
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/6e5f0d2118e441349f25a2bde1c8e4d9
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