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...
Enregistré dans:
Auteurs principaux: | Tobias Werther, Stefan Wahlefeld, Johannes Salewski, Uwe Kuhlmann, Ingo Zebger, Peter Hildebrandt, Holger Dobbek |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2017
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/6e5f0d2118e441349f25a2bde1c8e4d9 |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Flavin-dependent halogenases catalyze enantioselective olefin halocyclization
par: Dibyendu Mondal, et autres
Publié: (2021) -
Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
par: Max Willistein, et autres
Publié: (2019) -
A biomimetic redox flow battery based on flavin mononucleotide
par: Akihiro Orita, et autres
Publié: (2016) -
MSMEG_3955 from Mycobacterium smegmatis is a FMN bounded homotrimeric NAD(P)H:Flavin mononucleotide (FMN) oxidoreductase
par: Neha Khosla, et autres
Publié: (2021) -
Genomic Determinants Encode the Reactivity and Regioselectivity of Flavin-Dependent Halogenases in Bacterial Genomes and Metagenomes
par: Jehyun Jeon, et autres
Publié: (2021)