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...
Saved in:
Main Authors: | Tobias Werther, Stefan Wahlefeld, Johannes Salewski, Uwe Kuhlmann, Ingo Zebger, Peter Hildebrandt, Holger Dobbek |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2017
|
Subjects: | |
Online Access: | https://doaj.org/article/6e5f0d2118e441349f25a2bde1c8e4d9 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Flavin-dependent halogenases catalyze enantioselective olefin halocyclization
by: Dibyendu Mondal, et al.
Published: (2021) -
Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors
by: Max Willistein, et al.
Published: (2019) -
A biomimetic redox flow battery based on flavin mononucleotide
by: Akihiro Orita, et al.
Published: (2016) -
MSMEG_3955 from Mycobacterium smegmatis is a FMN bounded homotrimeric NAD(P)H:Flavin mononucleotide (FMN) oxidoreductase
by: Neha Khosla, et al.
Published: (2021) -
Genomic Determinants Encode the Reactivity and Regioselectivity of Flavin-Dependent Halogenases in Bacterial Genomes and Metagenomes
by: Jehyun Jeon, et al.
Published: (2021)