PMID: 6405789Jun 15, 1983Paper

Modification of cytochrome P-450 with fluorescein isothiocyanate

Biochimica Et Biophysica Acta
R BernhardtK Ruckpaul

Abstract

Fluorescein isothiocyanate (FITC) has been shown to be selectively attached to the N-terminus of cytochrome P-450 LM2. The N-demethylase activity of cytochrome P-450 LM2 reconstituted systems modified in this way was inhibited by 25%. As revealed by CD measurements the overall conformation as well as the immediate heme environment of cytochrome P-450 LM2 remained unchanged after attachment of the FITC molecule. The binding affinity of modified cytochrome P-450 LM2 toward benzphetamine and aniline and the cumene hydroperoxide- or H2O2-supported N-demethylation of benzphetamine are maintained. However, the introduction of the electron via NADPH-cytochrome P-450 reductase (EC 1.6.2.4) is impaired after modification of the alpha-amino group. The extent of reduced modified cytochrome P-450 LM2 in the cytochrome P-450 reductase-supported reduction reaction is diminished and the half-time of the reduction is increased. The diminished reducibility is ascribed to steric hindrance of groups directly involved in the interaction between cytochrome P-450 LM2 and NADPH-cytochrome P-450 reductase or to blocking of the charge-pair interactions between the alpha-amino group of P-450 LM2 and the respective negatively charged group of NADPH-cytoc...Continue Reading

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Citations

Jan 1, 1990·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·M J López-ZabalzaE Santiago
Sep 18, 2001·European Journal of Biochemistry·P Hlavica, D F Lewis
May 16, 1988·European Journal of Biochemistry·L MillerE Reisler
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