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

Bankala Krishnarjuna | Zendy; Toshio Yamazaki | Zendy; G.M. Anantharamaiah | Zendy; Ayyalusamy Ramamoorthy | Zendy

Open Access

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

Author(s) -

Bankala Krishnarjuna,

Toshio Yamazaki,

G.M. Anantharamaiah,

Ayyalusamy Ramamoorthy

Publication year - 2021

Publication title -

chemical communications

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.837

H-Index - 333

eISSN - 1364-548X

pISSN - 1359-7345

DOI - 10.1039/d1cc01018b

Subject(s) - flavin mononucleotide , flavin group , chemistry , reductase , flavoprotein , stereochemistry , biochemistry , enzyme

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.

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