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(Received for publication, June 11, 1996, and in revised form, July 16, 1996)
From the Departments of A microsomal cytochrome
b5 cDNA from the house fly, Musca
domestica, was cloned and sequenced. The deduced amino acid
sequence of the full-length house fly cytochrome
b5 (134 residues) is 48% identical to that of
rat microsomal cytochrome b5. The house fly
cytochrome b5 protein was overexpressed in
Escherichia coli, purified, and characterized. Absorption
and EPR spectroscopy reveal properties very similar to cytochromes
b5 from vertebrates. NMR spectra indicate that
the orientation of the heme in the protein relative to its
Volume 271, Number 43,
Issue of October 25, 1996
pp. 26637-26645
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Entomology and
§ Chemistry, University of Arizona, Tucson, Arizona
85721
,
meso axis is about 1:1. A redox potential of 
26 mV
versus standard hydrogen electrode was measured by cyclic
voltammetry on a modified gold electrode in the presence of
hexamminechromium(III) chloride. The cytochrome
b5 is reduced by house fly cytochrome P450
reductase in a reconstituted system at a high rate (5.5 s
1), and it stimulates heptachlor epoxidation when
reconstituted with house fly cytochrome P450 reductase, cytochrome P450
6A1, phospholipid, and detergent. Cytochrome b5
decreases the apparent Km for P450 reductase and
increases the Vmax for heptachlor epoxidation
at constant cytochrome P450 6A1 concentrations. The results indicate
that cytochrome b5 stimulates a step following
the first electron transfer during cytochrome P450 6A1 turnover.
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