Detergent-free isolation of CYP450-reductase's FMN-binding domain in E. coli lipid-nanodiscs using a charge-free polymer

Bankala Krishnarjuna; Thirupathi Ravula; Ayyalusamy Ramamoorthy

doi:10.1039/d1cc07193a

Detergent-free isolation of CYP450-reductase's FMN-binding domain in E. coli lipid-nanodiscs using a charge-free polymer

Chem Commun (Camb). 2022 Apr 14;58(31):4913-4916. doi: 10.1039/d1cc07193a.

Authors

Bankala Krishnarjuna¹, Thirupathi Ravula¹, Ayyalusamy Ramamoorthy¹

Affiliation

¹ Biophysics Program, Department of Chemistry, Macromolecular Science and Engineering, Biomedical Engineering, The University of Michigan, Ann Arbor, MI 48109-1055, USA. ramamoor@umich.edu.

Abstract

The membrane-anchored flavin mononucleotide binding domain (FBD) of CYP450 reductase was extracted in E. coli lipid-nanodiscs using charge-free pentyl-inulin polymer. FBD in nanodiscs was found to be conformationally homogenous and enabled high-resolution NMR probing. ³¹P NMR revealed the polymer's lack of preference for any specific E. coli lipids and identified the lipid-types in nanodiscs.

MeSH terms

Cytochrome P-450 Enzyme System
Escherichia coli / metabolism
Flavin Mononucleotide / chemistry
Lipid Bilayers / chemistry
Lipids
Nanostructures* / chemistry
Polymers* / chemistry

Substances

Lipid Bilayers
Lipids
Polymers
Flavin Mononucleotide
Cytochrome P-450 Enzyme System

Abstract

MeSH terms

Substances

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