Forster Distances of Ligand-Heme Pairs in Cytochrome P450 3A4

Details Forster Distances of Ligand-Heme Pairs in Cytochrome P450 3A4 Forster Distances of Ligand-Heme Pairs in Cytochrome P450 3A4

Apr 2003

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2003aps..apr.d1022f&link_type=abstract

American Physical Society, April Meeting, 2003, April 5-8, 2003 Philadelphia, Pennsylvania, MEETING ID: APR03, abstract #D1.022

Physics

Scientific paper

Cytochrome P450 3A4 is a protein in the human intestine and liver which oxidizes over half of drugs in use today. Cytochrome P450 3A4 has proven resistant to structure determination by NMR or x-ray crystallography. Fluorescence Resonance Energy Transfer (FRET) studies of P450 3A4 can be used to compute distances between fluorophores in the protein, providing information on the structure of the protein. For a ligand to be suitably used as a probe its fluorescence must not be completely quenched by the heme cofactor in P450 3A4. By using quantum yields, fluorescence, and the absorption spectra of six P450 ligands, the following Forster distances between each ligand and the P450 heme moiety were obtained: pyrene 4.6 nm, aflatoxin B2 5.7 nm, alpha-naphthoflavone 3.7 nm, indinavir 2.6 nm, quinidine 3.5 nm, and terfenadine 2.8 nm. Having these distances should yield a better low-resolution cytochrome P450 3A4 structure. Using the Forster distances, FRET experiments on inter-ligand placement in P450 3A4 will be undertaken soon.

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