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Solution phase refinement of active site structure using 2D NMR and judiciously ¹³C-labeled cytochrome P450.

ABSTRACT: The Cytochrome P450 (CYP450) superfamily has been the subject of intense research for over six decades. Here the HU227 strain of E. coli, lacking the δ-aminolevulinic acid (δ-ALA) synthase gene, was employed, along with [5-¹³C] δ-ALA, in the heterologous expression of P450cam harboring a prosthetic group labeled with ¹³C at the four methine carbons (C_m) and pyrrole C_α positions. The product was utilized as a proof of principle strategy for defining and refining solution phase active site structure in cytochrome P450cam, providing proton-to-proton distances from ¹³C_mH to protons on bound substrate or nearby amino acid residues, using short mixing time 2D or 3D NOESY-HMQC methods. The results reveal the interesting finding tha

SUBMITTER: Usai R

PROVIDER: S-EPMC10725731 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature

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Solution phase refinement of active site structure using 2D NMR and judiciously ¹³C-labeled cytochrome P450.

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Solution phase refinement of active site structure using 2D NMR and judiciously 13C-labeled cytochrome P450.

OmicsDI is part of the ELIXIR infrastructure

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Solution phase refinement of active site structure using 2D NMR and judiciously ¹³C-labeled cytochrome P450.