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J. Biol. Chem., Vol. 269, Issue 44, 27401-27408, Nov, 1994
CM Jenkins and MR Waterman
Two soluble flavoproteins, purified from Escherichia coli cytosol and
identified as flavodoxin and NADPH-flavodoxin (ferredoxin) reductase
(flavodoxin reductase), have been found in combination to support the 17
alpha-hydroxylase activities of heterologously expressed bovine 17
alpha-hydroxylase cytochrome P450 (P450c17). Physical characteristics of
the two flavoproteins including absorbance spectra, molecular weights, and
amino-terminal sequences are identical with those reported previously for
E. coli flavodoxin and flavodoxin reductase. Flavodoxin reductase,
possessing FAD as a cofactor, is able to reconstitute P450c17 activities
only in the presence of flavodoxin, an FMN- containing protein, and
NAD(P)H. Reducing equivalents are utilized more effectively from NADPH than
NADH by flavodoxin reductase. E. coli flavodoxin binds P450c17 directly and
with relatively high affinity (apparent Ks approximately 0.2 microM) at low
ionic strength, as evidenced by a change in spin state of the P450c17 heme
iron upon titration with flavodoxin. This apparent spin shift is attenuated
at moderate ionic strengths (100-200 mM KCl). In addition, bovine P450c17
binds reversibly to flavodoxin Sepharose in an ionic strength-dependent
manner. These data implicate charge pairing as being important for the
interaction between flavodoxin and P450c17. We propose that the amino acid
sequence similarity between E. coli flavodoxin-flavodoxin reductase and the
putative FMN, FAD, and NAD(P)H binding regions of cytochrome P450 reductase
provides the basis for the reconstitution of P450c17 activities by this
bacterial system.
Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.
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