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Nanodisc reconstitution of flavin mononucleotide binding domain of cytochrome-P450-reductase enables high-resolution NMR probing.


ABSTRACT: Cytochrome-P450-reductase transfers electrons to cytochrome-P450 through its flavin mononucleotide binding domain (FBD). Despite the importance of membrane-anchoring for FBD function, studies have focused on its soluble domain lacking the transmembrane-domain. Here we demonstrate that the reconstitution of FBD in nanodiscs enables high-resolution NMR measurements and renders a stable conformation.

SUBMITTER: Krishnarjuna B 

PROVIDER: S-EPMC8136615 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature

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Nanodisc reconstitution of flavin mononucleotide binding domain of cytochrome-P450-reductase enables high-resolution NMR probing.

Krishnarjuna Bankala B   Yamazaki Toshio T   Anantharamaiah G M GM   Ramamoorthy Ayyalusamy A  

Chemical communications (Cambridge, England) 20210416 39


Cytochrome-P450-reductase transfers electrons to cytochrome-P450 through its flavin mononucleotide binding domain (FBD). Despite the importance of membrane-anchoring for FBD function, studies have focused on its soluble domain lacking the transmembrane-domain. Here we demonstrate that the reconstitution of FBD in nanodiscs enables high-resolution NMR measurements and renders a stable conformation. ...[more]

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