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J Am Chem Soc. 2005 Oct 12;127(40):13816-21.

Observation of ligand binding to cytochrome P450 BM-3 by means of solid-state NMR spectroscopy.

Author information

1
Department of Chemistry, Columbia University, 3000 Broadway, New York, New York 10027, USA.

Abstract

A broad understanding of the binding modes of ligands and inhibitors to cytochrome P450 is vital for the development of new drugs. We investigated ligand binding in a site-specific fashion on cytochrome P450 BM-3 from Bacillus megaterium, a 119 kDa paramagnetic enzyme, using solid-state magic angle spinning nuclear magnetic resonance methods. Selective labeling and longitudinal relaxation effects were utilized to identify the peaks in a site-specific fashion and to provide evidence for binding. Well-resolved one-dimensional and two-dimensional NMR spectra of cytochrome P450 BM-3 reveal shifts upon binding of its substrate, N-palmitoylglycine. These data are consistent with the crystallographic result that a biochemically important amino acid residue, Phe87, moves upon ligation. This experimental scheme provides a tool for probing ligand binding for complex systems.

PMID:
16201802
DOI:
10.1021/ja0438314
[Indexed for MEDLINE]

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