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6
Substrate Oxidation by Cytochrome
P450 Enzymes
Paul
R.
Ortiz de Montellano and James J. De Voss
1.
Introduction
The cytochromes P450
are
catalytic hemo-
proteins
in
which
the
heme iron atom
is
coordi-
nated to a proximal cysteine thiolate. This thiolate
ligand
is
responsible
for the
characteristic Soret
absorption maximum
of
the Fe"-CO complex
at
—450 nm and is critical for P450 catalysis^. Early
site-specific mutagenesis studies with CYP1A2
and
P450^^j^
suggested that replacement
of the
cysteine thiolate
by a
histidine ligand gave inac-
tive protein^' ^. Detailed studies
of the
P450^^^
Cys357His mutant have recently confirmed that
this mutant enzyme
has an
almost undetectable
catalytic activity^' ^.
The low
camphor-oxidizing
activity
is
paralleled by
a
low rate of reduction
of
the iron,
an
elevated autooxidation rate,
and an
observable peroxidase activity"*.
The
thiolate lig-
and
is
thus clearly critical
for
P450^^j^
function,
although
the
relative contributions
of the
elec-
tronic
vs
structural perturbations
of
the mutation
to the low catal)^ic activity remain unclear. These
results agree with the results
of
experiments with
thiolate ligated metalloporphyrin model systems^'
^
and
of
computational analyses
of
the role
of
the
thiolate (see Chapter
2)^'
^.
The heme iron ligand
on the
distal side
is a
water molecule
in all the
available crystal struc-
tures
of
substrate-free P450 enzymes, including
P450^^^ (CYPlOl)io,
P450B^.3
(CYP102)11'
'\
P450^^^p (CYP108)i3, P450^^yp (CYP107Al)l^
P450^^^
(CYP55Al)i^ Sulfolobus solfataricus
CYPl
19^^
Streptomyces coelicolor CYP154Cli\
Mycobacterium tuberculosis CYP52^^, Sorangium
cellulosum P450epoK^^,
and the
mammalian
CYP2C5 (see Chapter
3>f^.
Although the thiolate
ligand
is
always present,
the
distal water ligand
appears
to be
absent
in
some mammalian
enzymes, either because the water does not bind in
those structures
or
because
it is
displaced
by an
endogenous ligand^ ^
The c)^ochrome P450 catalytic cycle is initiated
by
the
binding
of a
substrate, usually with con-
comitant displacement
of
the distal water ligand.
The ferric heme is then reduced to the ferrous state
using electrons provided by suitable electron donor
proteins
(see
Chapter 4).
In
cytochrome P450^^
and many other P450 enzymes, substrate binding
is widely believed to be a prerequisite for the trans-
fer
of
the first electron
to the
iron,
but in
some
enzymes electron transfer
can
occur without
the
prior binding of a substrate^
^.
Reduction of the iron
is followed by binding
of
oxygen
to
give
the
fer-
rous dioxy complex. Transfer of
a
second electron
to this complex produces
the
ferric peroxy anion
(PorFe"^-00~, where Por
=
porphyrin)
or,
after
protonation,
the
ferric hydroperoxo complex
(Por"^-OOH) (Figure 6.1). Heterolytic cleavage
of
Paul
R.
Ortiz
de
Montellano
•
Department
of
Pharmaceutical
Chemistry,
University
of
California,
San
Francisco,
CA.
James
J. De
Voss
•
Department
of
Chemistry,
University
of
Queensland,
Brisbane,
QLD
Australia.
Cytochrome
P450:
Structure,
Mechanism,
and
Biochemistry,
3e,
edited
by
Paul
R.
Ortiz
de
Montellano
Kluwer
Academic
/
Plenum
Publishers,
New
York,
2005.
183