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J Biol Chem, Vol. 274, Issue 33, 22999-23005, August 13, 1999
From the Department of Biochemistry, Emory University Medical
School, Atlanta, Georgia 30322 and the Department of
Biochemistry, Aichi Medical University, Nagakute,
Aichi 480-1195, Japan
An activation domain in p67phox (residues
within 199-210) is essential for cytochrome
b558-dependent activation of NADPH
superoxide (O
The p67phox Activation Domain Regulates Electron Flow
from NADPH to Flavin in Flavocytochrome
b558
2) generation in a cell-free system (Han, C.-H.,
Freeman, J. L. R., Lee, T., Motalebi, S. A., and
Lambeth, J. D. (1998) J. Biol. Chem. 273, 16663-16668). To determine the steady state reduction flavin in the
presence of highly absorbing hemes,
8-nor-8-S-thioacetamido-FAD ("thioacetamido-FAD") was
reconstituted into the flavocytochrome, and the fluorescence of its
oxidized form was monitored. Thioacetamido-FAD-reconstituted cytochrome
showed lower activity (7% versus 100%) and increased steady state flavin reduction (28 versus <5%) compared
with the enzyme reconstituted with native FAD. Omission of
p67phox decreased the percent steady state reduction of the
flavin to 4%, but omission of p47phox had little effect. The
activation domain on p67phox was critical for regulating flavin
reduction, since mutations in this region that decreased O2
generation also decreased the steady state reduction of flavin. Thus,
the activation domain on p67phox regulates the reductive
half-reaction for FAD. This reaction is comprised of the binding of
NADPH followed by hydride transfer to the flavin. Kinetic deuterium
isotope effects along with Km values permitted
calculation of the Kd for NADPH.
(R)-NADPD but not (S)-NADPD showed kinetic
deuterium isotope effects on V and V/K of about
1.9 and 1.5, respectively, demonstrating stereospecificity for the
R hydride transfer. The calculated Kd
for NADPH was 40 µM in the presence of wild type
p67phox and was ~55 µM using the weakly
activating p67phox(V205A). Thus, the activation domain of
p67phox regulates the reduction of FAD but has only a small
effect on NADPH binding, consistent with a dominant effect on
hydride/electron transfer from NADPH to FAD.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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