Mechanisms of peroxidase oxidation of o-dianisidine, 3,3′,5,5′- tetramethylbenzidine, and o-phenylenediamine in the presence of sodium dodecyl sulfate

Article abstract of DOI:10.1134/S1068162006010079

Peroxidase oxidation of o-dianisidine, 3,3′,5,5′- tetramethylbenzidine, and o-phenylenediamine in the presence of sodium dodecyl sulfate (SDS), an anionic surfactant, was spectrophotometrically studied. It was found that 0.1-100 mM SDS concentrations stabilize intermediates formed in the peroxidase oxidation of these substrates. The cause of the stabilization is an electrostatic interaction between positively charged intermediates and negatively charged surfactant. Pleiades Publishing, Inc., 2006.

Full text of DOI:10.1134/S1068162006010079

ISSN 1068-1620, Russian Journal of Bioorganic Chemistry, 2006, Vol. 32, No. 1, pp. 71–77. © Pleiades Publishing, Inc., 2006.
Original Russian Text © A.V. Kireyko, I.A. Veselova, T.N. Shekhovtsova, 2006, published in Bioorganicheskaya Khimiya, 2006, Vol. 32, No. 1, pp. 80–86.
Mechanisms of Peroxidase Oxidation of o-Dianisidine,
3,3',5,5'-Tetramethylbenzidine, and o-Phenylenediamine
in the Presence of Sodium Dodecyl Sulfate
1
A. V. Kireyko, I. A. Veselova, and T. N. Shekhovtsova
Faculty of Chemistry, Moscow State University, Vorob’evy gory, Moscow, 119992 Russia
Received June 29, 2005; in final form, August 10, 2005
Abstract—Peroxidase oxidation of o-dianisidine, 3,3',5,5'-tetramethylbenzidine, and o-phenylenediamine in
the presence of sodium dodecyl sulfate (SDS), an anionic surfactant, was spectrophotometrically studied. It was
found that 0.1–100 mM SDS concentrations stabilize intermediates formed in the peroxidase oxidation of these
substrates. The cause of the stabilization is an electrostatic interaction between positively charged intermediates
and negatively charged surfactant.
Key words: o-dianisidine; horseradish peroxidase, oxidation mechanism; o-phenylenediamine; sodium dodecyl
sulfate; 3,3',5,5'-tetramethylbenzidine
DOI: 10.1134/S1068162006010079
1
INTRODUCTION
and PDA oxidation with hydrogen peroxide catalyzed
by horseradish peroxidase.
The study of enzyme properties in surfactant solu-
tions [1, 2] is one of topics of numerous long-term
(since the end of the 1940s) investigations of enzyme
RESULTS AND DISCUSSION
2
behavior in aqueous media. The processes involved in
A Mechanism of the Peroxidase Oxidation of DA
in the Presence of SDS
the formation of protein–surfactant complex and the
effect of surfactant on the protein structure have been
thoroughly studied. In most cases, the same surfactant,
SDS, was used for studying the surfactant-induced pro-
tein denaturation [3–5].
It is well known that bisazobiphenyl is a stable prod-
uct of peroxidase oxidation of DA [11]. This product is
formed by coupling of two quinonediimine molecules
and has brown color (λmax 453–475 nm) (Scheme 1).
The oxidation of DA was established to proceed
through the formation of a green intermediate, to which
a meriquinoid structure (λmax 386 and 704 nm) was
assigned. The long-wavelength absorption band indi-
cates a probable charge-transfer interaction in the
meriquinoid complex [13]. According to [12], quinone-
diimine reversibly interacts with DA with the formation
of complex, and this equilibrium is sensitive to pH of
the reaction medium and the concentration of its com-
ponents.
It has been proposed that the action of surfactants on
proteins is determined by the van der Waals interactions
between organic moieties of surfactant molecules and
lyophylic protein groups [6]. The effects of charge dis-
tribution are also important [7]. Surfactants were found
to weaken hydrophobic interactions within the protein
molecule, not competing with peptide groups for
hydrogen bond formation [8]. At the same time, the
binding of surfactant may result in the breakage of
hydrogen bonds in protein because of destabilization of
its helical structure upon the interaction of surfactant
with the side chains of protein molecule [9]. It has been
also noted [1, 10] that, due to such interactions, func-
tional groups in enzyme molecules become more
accessible to chemical reactions and, hence, surfactants
may affect the mechanism of classical enzymatic pro-
cesses.
At the same time, the available literature data indi-
cate the formation of free cation radicals in the peroxi-
dase oxidation of DA, which were detected by electron
paramagnetic resonance technique [14, 15]:
H3CO
OCH3
.
The goal of this work was the study of the effect of
anionic surfactant SDS on the mechanism of DA, TMB,
+
H2N
NH2
1
Corresponding author; phone: +7 (095) 939-3458; e-mail:
We applied spectrophotometry to study the effect of
anionic surfactant SDS (at the concentration range of
0.01–100 mM) on the chemistry of peroxidase oxida-
tion of DA. Previously, the optimal conditions for car-
kireyko@analyt.chem.msu.ru
2
Abbreviations: CMC, critical concentration of micelle formation;
DA, o-dianisidine; PDA, o-phenylenediamine; SDS, sodium
dodecyl sulfate; and TMB, 3,3',5,5'-tetramethylbenzidine.
71

72
KIREYKO et al.
H3CO
HN
OCH3
NH
H3CO
H2N
OCH3
NH2
H3CO
OCH3
NH
–2H+ – 2e
H3CO
H2N
OCH3
NH2
HN
λmax 386; 704 nm
H3CO
OCH3 H3CO
OCH3
NH2
H2N
N N
λmax 455 nm
Scheme 1. The reaction scheme of peroxidase oxidation of DA.
rying out this indicator reaction were determined: mediate product of DA oxidation (Fig. 1, curve 4). Note
0.2 nM peroxidase, 0.1 mM DA, 0.5 mM H2O2, and
0.1 M phosphate buffer (pH 5.5).
that, in the absence of SDS, the intermediate com-
pletely transforms into the main product 2 min after the
reaction start, whereas, in the presence of SDS at con-
centrations higher than 0.1 mM, the intermediate is
converted into the main product only after 15 min
(Fig. 2, curve 4). Such stabilization of the intermediate
product of the DA peroxidase oxidation in the presence
of SDS obviously confirms the opinion on the possibil-
ity of cation-radical formation. The stabilization may
take place only due to the interaction of a positively
charged component with premicellar and micellar
aggregates of the anionic surfactant that have a high
We found that SDS does not affect the course of the
indicator reaction at concentrations less than 0.1 mM,
and the absorption spectra of DA oxidation products are
practically the same in the presence and the absence of
SDS (Fig. 1, curves 1 and 1', 2 and 2'). Significant
changes in the absorption spectra of reaction products
were observed upon increasing SDS concentration in
the reaction mixture. At 1 mM SDS, the absorption
spectra registered 2 min after starting the reaction dis-
played maxima at 390 and 670 nm, which in fact corre-
sponded to the wavelengths characteristic of the inter- density of negative charges formed in aqueous solu-
A
A
1.2
1.2
4
2
4
1.0
0.8
0.6
0.4
1.0
0.8
0.6
0.4
3
1
5
1, 1', 2, 2'
3
0.2
0
5
3
0.2
0
300
400
500
600
700 nm
360
460
560
660
760 nm
Fig. 2. Absorption spectra of the products of the DA perox-
idase oxidation: (1) registered 2 min after mixing the reac-
tion components in the absence of SDS; (2, 3, and 4) regis-
tered 15 s, 10 min and 15 min, respectively, after mixing the
reaction components in the presence of 1 mM SDS. Con-
centrations of other components are indicated in the caption
to Fig.1; all reactions were carried out in 0.1 M phosphate
buffer (pH 5.5).
Fig. 1. Absorption spectra of the products of the peroxidase
oxidation of DA registered 2 min after mixing the reaction
components: (1, 2) in the absence of SDS; (1' and 2', 3, 4,
5) in the presence of 0.01, 0.1, 1, and 10 mM SDS, respec-
tively. Reaction conditions: 0.2 nM peroxidase, 0.1 mM
DA, 0.5 mM H O ; (1, 1', 3–5) 0.1 M phosphate buffer (pH
2
2
5.5); (2, 2') 0.1 M acetate buffer (pH 5.5).
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY Vol. 32 No. 1 2006

MECHANISMS OF PEROXIDASE OXIDATION
73
tions of the anionic surfactant (CMC of SDS is
1.53 mM in the phosphate buffer with pH 5.5 [16]).
A360
0.24
The replacement of anionic SDS with a cationic sur-
factant (cetyltrimethylammonium bromide) or a non-
ionic surfactant (Triton X-100 or Brij-35) results in the
disappearance of the stabilization of intermediate prod-
uct of DA oxidation and its absence. This confirms our
presumption on the existence of the electrostatic inter-
action of the positively charged cation radical with the
anionic surfactant.
Remember that the detected intermediate has green
color, which is characteristic of the intermediate
meriquinoid complex. All the above-described facts
indicate that the two compounds, the charge-transfer
complex and the cation radical, are at equilibrium in the
reaction mixture.
A further increase in the SDS concentration (to
10 mM) leads to the shift of absorption maxima corre-
sponding to the intermediate product of DA oxidation
from 390 to 380 nm and from 670 to 710 nm (Fig. 1,
curve 5). These spectral changes can be explained by a
stronger electrostatic interaction of the protonated
intermediate of DA oxidation with the concentrated
negative charge of direct SDS micelles at the concen-
trations exceeding CMC. In addition, the intensity of
optical absorption at these maxima was somewhat
decreased. The reason of these phenomena is probably
a partial denaturation of the enzyme under the action of
surfactant.
The effect of 1 mM SDS on this reaction was studied
in a broad range of pH values (pH 5,5–7.5 phosphate
buffer and pH 8.0–9.0 borate buffer) in order to prove
the electrostatic nature of SDS binding to the interme-
diate product formed during the peroxidase-catalyzed
oxidation of DA (Fig. 3). We found that SDS stabilizes
the intermediate at pH 5.5–7.0. At higher pH values, no
stabilization of the green product of DA oxidation was
observed; the isoelectric point of this peroxidase is 7.2.
The experiments were not carried out at pH values
lower than 5.0, since the catalytic activity of the perox-
idase is significantly reduced under these conditions.
We ascertained, whether the nature of the buffer
solution would affect the changes observed in the
absorption spectra of DA oxidation products in the
presence of SDS. The spectra registered in two buffer
solutions, pH 5.5–7.5 phosphate buffer and pH 5.5 ace-
tate buffer, containing SDS turned out to be identical
(Fig. 1, curves 1', 2'). This implies that the SDS-induced
stabilization of the intermediate product and the
changes observed in the positions of the absorption
maxima are not the consequences of the interaction of
this surfactant with the components of buffer solution.
We also verified, whether the peculiarities of perox-
idase oxidation of DA in the presence of SDS could be
explained by the biological nature of the catalyst. To
this end, the reaction was carried out in the presence of
an inorganic catalyst, Cr(VI) [17]. In this experiment,
0.20
0.16
0.12
2
1
0.08
0.04
0
5.0 5.5 6.0 6.5 7.0 7.5 8.0 8.5 9.0 9.5
pH
Fig. 3. Absorption of the intermediate product of the perox-
idase oxidation of DA (λ 360 nm) registered 15 s after start-
ing the reaction as a function of pH of 0.1 M phosphate (pH
5.5–7.5) and 0.1 M borate (pH 8–9) buffer solutions: (1) in
the absence of SDS; (2) in the presence of 1 mM SDS. Con-
centrations of other components are indicated in the caption
to Fig.1.
A
1.5
4
1.0
3
0.5
1
2
0
360
460
560
660
760 nm
Fig. 4. Absorption spectra of the products of the Cr(VI)-cat-
alyzed oxidation DA registered 2 min after mixing the reac-
tion components: (1) in the absence of SDS; (2, 3, and 4) in
the presence of 0.1, 1.0, and 10 mM SDS, respectively. Con-
ditions of the reaction: 1 µg/ml Cr(VI), 2.5 mM DA, 0.3 M
H O , 0.1 M acetate buffer (pH 5.5).
2
2
the concentrations exceeding 0.1 mM (Fig. 4) as in the
case of the enzymatic reaction. Moreover, as far as the
surfactant does not affect activity of the inorganic cata-
lyst, the absorption maxima corresponding to the inter-
mediate product continued to grow with increase in
SDS concentration to 10 mM, which discriminates this
process from the peroxidase oxidation of DA. Like in
the case of the enzymatic reaction, the absorption max-
imum corresponding to the intermediate product of DA
oxidation is somewhat shifted to the short-wave region
in the presence of chromium and 10 mM SDS.
The data led us to conclusion that the stabilization of
the intermediate product in the presence of SDS is not
related to the biological nature of the catalyst. The shift
of the absorption maximum of this product observed
with 10 mM SDS in the reaction carried out in the pres-
ence of both biological and inorganic catalyst evidently
results from a more effective interaction of the interme-
SDS stabilized the intermediate when being added at diate product with SDS aggregates formed in micelles.
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY Vol. 32 No. 1 2006

74
KIREYKO et al.
.
+
H3C
CH3
NH2
CH3
H3C
H2N
H3C
CH3
NH2
CH3
–e–
H2N
H3C
H3C
H2N
CH3
NH2
H3C
HN
H3C
CH3
NH
–e–
H3C
H3C
CH3
CH3
+ H+
1/2
CH3
HN
H3C
NH
λmax 465 nm
CH3
max 375; 655 nm
λ
Scheme 2. The reaction scheme of peroxidase oxidation of TMB.
Mechanism of the Peroxidase Oxidation of TMB
in the Presence of SDS
bilize the intermediate product of TMB oxidation. This
presumption was confirmed by carrying out this indica-
tor reaction under optimal conditions (0.2 nM peroxi-
dase. 40 µM TMB, 0.2 mM hydrogen peroxide, pH 5.5)
in the presence of SDS at the concentration exceeding
0.1 mM (Fig. 5). Interestingly, the stabilization is so
strong that the intermediate does not transform into the
main product even after 2 days of incubation of the
reaction mixture (Fig. 5, curve 5).
A study of the peroxidase oxidation of TMB has
shown that the product of one-electron oxidation of this
substrate is a cation radical (Scheme 2), which is in
equilibrium with a meriquinoid complex of blue color
(λmax 375 and 655 nm [15]. A kinetic study of the per-
oxidase-catalyzed oxidation of TMB confirmed the for-
mation of free cation radicals [18]. The final product of
the TMB oxidation is quinonediimine of yellow color
(λmax 465 nm).
The Mechanism of the Peroxidase Oxidation of PDA
in the Presence of SDS
A similarity in the mechanisms of DA and TMB
oxidation allowed us to presume that SDS will also sta-
It is known [19] that the final product of PDA oxida-
tion is 2,3-diaminophenazine of yellow-orange color
(λmax 420–450 nm) (Scheme 3) [20]. We found optimal
conditions for the horseradish peroxidase–catalyzed
PDA oxidation: 0.2 nM peroxidase, 0.3 mM PDA,
0.3 mM hydrogen peroxide, pH 5.5. Figure 6 (curve 1)
shows the results of spectrophotometric study of this
reaction. At a deficiency of the oxidant substrate ç2é2
(the ratio of the concentrations of reducing agent and
oxidant is 10 : 1), a maximum corresponding to the
intermediate product of PDA oxidation (380 nm)
becomes first apparent in the absorption spectrum of
reaction products (Fig. 6, curve 2). With time, this max-
imum transforms to the maximum of the main product.
A presumable structure of the intermediate product of
peroxidase oxidation of PDA is presented in Scheme 3
[21].
A
1.5
1, 2
1.0
3, 5
3, 5
0.5
0
4
4
300
400
500
600
700 m,
Fig. 5.Absorption spectra of products of the peroxidase oxi-
dation of TMB registered 2 min after mixing the reaction
components: (1) in the absence of SDS; (2, 3, and 4), in the
presence of 0.01, 1, and 10 mM SDS; (5) registered after
2 days in the presence of 1 mM SDS. Reaction conditions:
0.2 nM peroxidase, 40 µM TMB, 0.2 mM H O , 0.1 M
A study of the peroxidase oxidation of PDA in the
presence of SDS in a phosphate buffer, pH 5.5–7.5,
2
2
phosphate buffer (pH 5.5).
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY Vol. 32 No. 1 2006

MECHANISMS OF PEROXIDASE OXIDATION
NH
75
NH2
NH
NH
max 380 nm
N
NH2
NH2
NH
[O]
NH2
N
λ
λ
max 450 nm
Scheme 3. The reaction scheme of peroxidase oxidation of PDA.
showed that three maxima were present in the absorp-
A study of the PDA oxidation in the presence of
tion spectrum of the reaction products at the SDS con- SDS and inorganic catalyst Fe(III) under the conditions
centration exceeding 1 mM. These were a broad maxi- optimized in [22] showed that, as with the enzymatic
reaction, the intermediate product is formed at the SDS
concentration exceeding 1 mM, and the absorption
maximum of the main product was somewhat shifted to
the long wavelength region (Fig. 8). Thus, the effect of
SDS on the chemistry of this indicator reaction also
does not depend on the nature of catalyst.
mum in the region of 550–650 nm, a sharp maximum at
365 nm, and a maximum presumably corresponding to
the main product of PDA oxidation but shifted from
430 to 455 nm (Fig.6, curves 3, 4). In this case, the solu-
tion has a green color. With time, the height ratio of
absorption maxima of the final and intermediate prod-
ucts significantly increases (Fig. 7). The intermediate
product completely transforms into the main product
only after 10 min.
CONCLUSIONS
The oxidation of three peroxidase substrates, DA,
PDA, and TMB, in the presence of SDS was studied. It
was found that 0.1–100 mM SDS stabilizes the inter-
mediate positively charged oxidation products. Electro-
static interactions of these products with negatively
charged SDS are apparently responsible for this stabili-
zation.
Our results are interesting not only for understand-
ing the mechanism of the above-mentioned reactions in
aqueous surfactant solutions, but also for the prospec-
tive application of these reactions to chemical analysis.
The addition of surfactants to the indicator reaction
In the absence of SDS, the intermediate product of
PDA oxidation is obviously transformed into the main
product so quickly that it is practically impossible to
detect its formation under the optimal reaction condi-
tions. In the presence of SDS, the intermediate product
is stabilized due to the formation of ionic associate with
this anionic surfactant.
The electrostatic nature of bonds between the inter-
mediate product and the anionic surfactant was proved
by studying the peroxidase oxidation of PDA in the
presence of 5 mM SDS in borate buffer, pH 8.0–10.0.
We found that, like the oxidation of DA, the oxidation allows one to affect the process in order to select the
of PDA in alkaline medium do not lead to the interme- step most suitable for analytical purposes. For example,
diate product (data not shown).
the formation rate of the green intermediate product of
A
A
0.8
4
0.7
0.6
0.5
0.4
3
0.6
0.4
1
1
3
2
0.3
0.2
0.1
0
0.2
2
2
400
3
0
300
500
600
700nm
300
400
500
600
700 nm
Fig. 7.Absorption spectra of products of the peroxidase oxi-
dation of PDA: (1) registered 2 min after mixing the com-
ponents in the absence of SDS; (2) registered 2 min after
mixing the components in the presence of 5 mM SDS;
(3) registered 5 min after mixing the components in the
presence of 5 mM SDS. The concentrations of other com-
ponents are indicated in the caption to Fig. 6. The reactions
were carried out in 0.1 M phosphate buffer (pH 5.5).
Fig. 6.Absorption spectra of products of the peroxidase oxi-
dation of PDA registered 2 min after mixing the reaction
components: (1, 2) in the absence of SDS; (3, 4) in the pres-
ence of 5 and 10 mM SDS. The reaction conditions: 0.2 nM
peroxidase, (1, 3, 4) 0.3 mM PDA and (2) 3 mM PDA,
0.3 mM H O , 0.1 M phosphate buffer (pH 5.5).
2
2
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY Vol. 32 No. 1 2006

76
KIREYKO et al.
hydrogen peroxide, was determined by titration with
permanganate.
A
1.0
The rate of indicator reactions of DA, PDA, and
TMB oxidation was monitored by spectrophotometry
by increase in the optical density of solutions (A) owing
to the accumulation of colored products. It was charac-
4
3
0.5
0
terized by a slope (tanα ) of kinetic curves in the opti-
cal density–time coordinates. The optical density and
the absorption spectra were registered using a UV-2201
spectrophotometer (Shimadzu, Japan).
Distilled water was purified on a Simplicity appara-
tus (Millipore, France) to a specific resistance no less
than 18 megohm/cm and used for preparation of all
aqueous solutions.
The reactions of DA, PDA, and TMB oxidation with
hydrogen peroxide in the presence of horseradish per-
oxidase were carried out according to the following
procedure. A buffer solution (required volume), 10 nM
peroxidase (0.1 ml), reducing substrate (0.1 ml of 5, 15,
or 2 mM solution of DA, PDA, and TMD, respectively),
and hydrogen peroxide (0.1 ml of 25, 15, or 10 mM
solution for DA, PDA, and TMD, respectively) were
successively added to a test tube with a ground-glass
stopper. The total volume of the reaction mixture was
5 ml. After addition of hydrogen peroxide, the solution
was stirred, and a stopwatch was simultaneously
switched on. The solution was placed in a quartz
cuvette (l 1 cm) and absorption spectra of oxidation
products were registered at certain intervals.
1, 2
330
430
530
630
730nm
Fig. 8. Absorption spectra of products of the Fe(III)-cata-
lyzed oxidation of PDA registered 2 min after mixing the
components: (1) in the absence of SDS; (2, 3, 4) in the pres-
ence of 0.1, 1, and 10 mM SDS, respectively. The reaction
conditions: 40 µM Fe(III), 7.5 mM PDA, 0.3 mM H O ,
2
2
0.1 M phosphate buffer (pH 5.5).
DA oxidation catalyzed by peroxidase is significantly
higher in the presence of 1 mM SDS (pH 5.5) than the
rate of formation of the main product under the same
conditions but in the absence of SDS. This property can
be used for increasing the sensitivity of procedures
used for the determination of various compounds,
which can be second substrates or effectors of the per-
oxidase. For the purpose of identification and quantita-
tive determination of effectors of this enzyme, the rate
of TMB oxidation can be monitored by accumulation
of not only the final product (λmax 465 nm), but also the
intermediate compound with λmax 375 nm; this can be
preferable in some cases.
The indicator reactions in the presence of SDS were
carried out according to the procedure described above,
except for addition of a SDS solution (0.1 ml) of
required concentration to the reaction mixture after
adding peroxidase.
EXPERIMENTAL
ACKNOWLEDGMENTS
A dry preparation of horseradish peroxidase (EC
1.11.1.7) (Merck, Germany) was used to prepare solu-
tions in 0.05 M phosphate buffer (pH 7.0). The specific
activity of the enzyme was 192 U/mg. The precise con-
centration of peroxidase was determined spectrophoto-
metrically (ε403 9.4 × 104 å–1 cm–1 [23]). The dry per-
oxidase preparation and its aqueous solutions were
stored at 4°ë.
This work was supported by the Russian Foundation
for Basic Research, project no. 04-03-33116.
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