Distance between lysine 384 and heme of cytochrome P-450 LM2 (P-450 IIB4) studied by fluorescence energy transfer measurements

Biochemical and Biophysical Research Communications
R BernhardtK Ruckpaul

Abstract

The distance between FITC-modified lysine 384 of cytochrome P-450 LM2 and the active site, heme, was estimated by fluorescence energy transfer measurements. To avoid differential labelling of P-450 LM2 for protection of the alpha-amino group from FITC modification, deconvolution of measured fluorescence decay curves using a double exponential model was performed. A value of 2.7 nm was obtained for the distance FITC (lysine 384) - heme. This distance is too large to account for a direct electron tunneling from prosthetic group to prosthetic group at this interaction site between reductase and P-450 LM2.

References

Jan 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·M J Potasek, J J Hopfield
Jun 15, 1983·Biochimica Et Biophysica Acta·R BernhardtK Ruckpaul
May 31, 1983·Biochemical and Biophysical Research Communications·W SchwarzeK Ruckpaul
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Oct 1, 1984·Archives of Biochemistry and Biophysics·G T Miwa, A Y Lu
Nov 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·G E TarrM J Coon

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Citations

Nov 24, 1999·Biochemical and Biophysical Research Communications·J A García-BarradoP Macías
Jun 1, 1992·Journal of Computer-aided Molecular Design·D F Lewis, H Moereels
Jan 22, 1998·Free Radical Biology & Medicine·C A Metosh-DickeyG W Winston
Apr 1, 1995·Xenobiotica; the Fate of Foreign Compounds in Biological Systems·D F Lewis
Jan 1, 1993·Drug Metabolism Reviews·L KoymansN P Vermeulen

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