in situ from hydration of 5-chloro-N7-methylUA in potas-
sium phosphate buffer.17 2-Methyl-Spd (minor product) and
3-methyl-Alla (major product) were isolated from the
decomposition of 5-chloro-N7-methylUA as well as from
the oxidation of N7-methylUA by Na2IrCl6. This unambigu-
ously demonstrates that these two compounds are products
of 5-OH-N7-methylUA in the oxidation of N7-methylUA
and strongly suggests that Spd and Alla are products of
5-OH-UA in the oxidation of UA.
Table 2. Summary of Oxidation of UA by ONOO- and
Enzyme-mediated Oxidantsa
ONOO-
(equiv)
Sp d (%) Alla (%) enzyme Sp d (%) Alla (%)
0.2
0.5
1.0
2.0
10
nd
nd
0.09
0.14
0.06
0.14
3
8
12
16
nd
nd
1
2
3
4
5
0.04
0.04
0.06
0.07
0.006
8
10
21
19
56
Formation of analogous intermediates and similar pH
dependence of formation of the spiro compounds suggest
that the oxidation of UA and 8-oxoG share similar pathways
(Scheme 1). The significant difference between the yields
20
a Nd ) not detectable.
oxidation was carried out in pH 7.2 potassium phosphate
and sodium bicarbonate buffer via bolus addition of ONOO-.
The yield of Alla was <16% when < 2 equiv of ONOO-
were used and not detectable at >10 equiv of ONOO-
treatment. The formation of Spd (∼0.1% yield) showed no
significant dose response. In the uricase/O2 oxidation, the
yield of Alla was 56%, while the yield of Spd (0.006%)
was significantly lower than that in oxidation of UA by Na2-
IrCl6. In the HRP- or MPO-mediated oxidation, the yields
of Alla and Spd were in the range of 8-21% and 0.04-
Scheme 1. Decomposition of 5-OH-UA and 5-OH-8-oxoG
-
0.07%, respectively, and did not differ significantly if NO2
was present, suggesting no significant oxidation by NO2.
Control experiments with no addition of ONOO- or enzymes
were carried out to ensure no false positive formation of Spd.
To confirm that Spd and Alla and Sp and Gh bases are
products of 5-OH-UA and 5-OH-8-oxoG intermediates,
respectively, we carried out oxidation of UA and 8-oxoG
by Na2IrCl6 both in H216O and H218O (95% enriched) in pH
9.5 phosphate buffer. The isolated Spd, Alla, Sp, and Gh
bases were analyzed by ESI-TOF MS in negative ion mode,
and those reactions done in H216O gave [M - H]- at 183.0,
157.0, 182.0, and 156.1, respectively. From oxidation in
H218O, [M - H]- ions at 185.0, 159.0, 184.0, and 158.1 were
observed (see Supporting Information), suggesting that the
OH group in 5-OH-UA and 5-OH-8-oxoG comes from water
and that the oxygen atom is retained in the products. This
supports the intermediacy of 5-OH-UA and 5-OH-8-oxoG.
The definitive proof that Spd is a product of 5-OH-UA
would require independent synthesis of 5-OH-UA and
isolation of Spd from its decomposition. Because 5-OH-
UA is very unstable, we used 5-OH-N7-methylUA as its
surrogate because oxidations of UA and N7-methylUA
proceed via similar intermediates, namely, 5-OH-UA and
5-OH-N7-methylUA.16 5-OH-N7-MethylUA was generated
of Spd and Sp base is very intriguing. The absence of
significant formation of 1-methyl-Spd (<9% yield) from
oxidation of N9-methylUA by Na2IrCl6 excluded the role
of N9-substituents in causing the low yield of Sp. The
transient existence of 5-OH-UA and 5-OH-8-oxoG has
limited efforts to probe their decomposition mechanism.
However, the physicochemical properties of stable analogues
suggest that deprotonation of 5-OH facilitates the formation
of spiro compounds via pathway II,18,19 and enolization of
the C6 carbonyl slows the hydrolysis of the N1-C6 amide
bond and pathway I.20
On the basis of observations from Burrows21,22 and our
group,23 we propose pathways I and II (Scheme 1) to be
competitive. The predominant form of 5-OH-UA in pH range
7-11 is the N9-deprotonated species (1)5,24 (Scheme 2),
while the predominant form of 5-OH-8-oxoG is the neutral
species (4)25 at pH 7. At pH ∼ 10, N9 of 5-OH-8-oxoG is
deprotonated (6) (N9 pKa ∼ 9 using structural similarity
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Org. Lett., Vol. 6, No. 19, 2004
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