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Stoichiometry of 7‐ethoxycoumarin metabolism by cytochrome P450 2B1 wild‐type and five active‐site mutants
Author(s) -
Fang Xiaojun,
Kobayashi Yasuna,
Halpert James R
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01173-3
Subject(s) - mutant , cytochrome p450 , wild type , chemistry , substrate (aquarium) , metabolism , binding site , cytochrome , recombinant dna , biochemistry , stoichiometry , active site , enzyme , biology , gene , ecology , organic chemistry
Recombinant P450 2B1 wild‐type and the active‐site mutants I114V, F206L, V363A, V363L, and G478S were purified and studied. The efficiency of coupling of reducing equivalents to 7‐hydroxycoumarin formation was decreased for all the mutants except I114V. Uncoupling to H 2 O was increased for F206L, V363A, and G478S, decreased for V363L, and unchanged for I114V. Uncoupling to H 2 O 2 was increased for V363L and decreased for I114V, F206L, and V363A. The findings from this study provide firm biochemical evidence that residues 206, 363, and 478 comprise part of the substrate binding site of P450 2B1.