Oxidase-like MOF-818 Nanozyme with High Specificity for Catalysis of Catechol Oxidation

Article abstract of DOI:10.1021/jacs.0c07273

Despite the extensive studies of the nanozymes showing their superior properties compared to natural enzymes and traditional artificial enzymes, the development of highly specific nanozymes is still a challenge. The catechol oxidase specifically catalyzing the oxidations of o-diphenol to the corresponding o-quinone is important to the biosynthesis of melanin and other polyphenolic natural products. In this study, we first propose that MOF-818, containing trinuclear copper centers mimicking the active sites of natural catechol oxidase, shows efficient catechol oxidase activity with good specificity and no peroxidase-like characteristics. MOF-818 has good specificity and high catalytic activity as a novel catechol oxidase nanozyme.

Full text of DOI:10.1021/jacs.0c07273

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Article
Oxidase-like MOF-818 Nanozyme with High
Specificity for Catalysis of Catechol Oxidation
Minghua Li, Jinxing Chen, Weiwei Wu, Youxing Fang, and Shaojun Dong
J. Am. Chem. Soc., Just Accepted Manuscript • DOI: 10.1021/jacs.0c07273 • Publication Date (Web): 13 Aug 2020
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Oxidase-like MOF-818 Nanozyme with High Specificity for Catalysis
of Catechol Oxidation
Minghua Li, § [a,b] Jinxing Chen, § [b,c] Weiwei Wu,[b,c] Youxing Fang, * [b] Shaojun Dong*[a,b,c]
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[a] College of Chemistry, Jilin University, Changchun, 130012, P.R. China.
[
b] State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of
Sciences, Changchun, 130022, P. R. China.
c] University of Science and Technology of China, Hefei, Anhui, 230026, P.R. China.
[
ABSTRACT: Despite the extensive studies of the nanozymes showing their superior properties compared to natural enzymes and
traditional artificial enzymes, the development of highly specific nanozymes is still a challenge. The catechol oxidase specifically
catalyzing the oxidations of o-diphenol to the corresponding o-quinone is important to the biosynthesis of melanin and other
polyphenolic natural products. In this study, we firstly propose that MOF-818, containing trinuclear copper centers mimicking the
active sites of natural catechol oxidase, shows the efficient catechol oxidase activity with good specificity and no peroxidase-like
characteristics. MOF-818 has good specificity and high catalytic activity as a novel catechol oxidase nanozyme.
INTRODUCTION
Polyphenol oxidases include tyrosinase and catechol
oxidase. In vivo, tyrosinase plays an important role in the
biosynthesis of melanin and other polyphenolic natural
Nanomaterials with enzymatic activities (nanozyme) have
been comprehensively investigated due to their high stability,
high catalytic efficiency, low price and conveniences of
3
7
products, while catechol oxidase catalyzes the oxidation of
substrates into corresponding o-quinones which can be
polymerized to produce melanin and form an insoluble barrier
1
-3
preparation.
Nanozymes are considered to be excellent
substitutes for natural enzymes.4 So far, a large number of
-6
38
to protect the damaged plant from pathogens or insects.
nanomaterials with enzyme-like activity have been discovered
and designed, including metals, metal oxides,
Since polyphenol oxidases have significant biological effects,
it is necessary to explore nanomaterials to mimic polyphenol
oxidases and their related catalytic mechanisms.
7
-8
9-11
metal-
1
2-16
organic frameworks (MOFs)
and carbon-based
1
7-18
materials.
According to the types of catalysis, nanozymes
19
20-21
In this work, we demonstrate that a MOF based
can be classified into oxidase mimic, peroxidase mimic,
22-23
24
nanomaterial, MOF-818, catalyzes the oxidation of catechols,
but shows no peroxidase-like activity. Moreover, by
mimicking the active center of natural catechol oxidase, MOF-
818 exhibits higher catalytic ability and specificity than the
reported oxidation nanozymes. 3,5-di-tert-butylcatechol (3,5-
DTBC) was selected as the substrate for studying catechol
oxidase activity because it has superior solubility and is
infeasible to be polymerized than other catechol derivatives.
MOF-818 exhibits the catalytic behaviors similar to natural
catechol oxidase, which is completely different from the
previously reported oxidase nanozymes. Natural catechol
oxidases, containing a coupled binuclear copper metal center
coordinated by six histidines as the active site, catalyzes the
superoxide dismutase mimic,
catalase mimic
and
25-26
hydrolase mimic,
etc. Due to the excellent performances of
nanozymes, various nanozymes have been extensively studied
2
7-28
for the applications of biosensors,
environmental
2
9
30
protections,
disease diagnosis and treatments,
and
3
1
antibacterial agents.
Despite the increasing interests in nanozymes, the
development of highly specific nanozymes is still a challenge.
Oxidase nanozyme has been widely studied as an important
topic of nanozymes, while the previously reported metal
oxides and noble metals based nanozymes applied to oxidase
mimics still show peroxidase-like activity, which merely use
3
,3',5,5'-tetramethylbenzidine (TMB) and 2,2'-azino-bis(3-
oxidation of o-diphenol, while O
2
is reduced to peroxide in the
ethylbenzothiazoline-6-sulfonic acid (ABTS) as universal
substrates. TMB and ABTS are typical substrates of
peroxidase to certify the peroxidase activity, and not qualified
to characterize oxidase activity. Currently, oxidase nanozymes
ternary enzyme–catechol–dioxygen complex, and then
3
9
protonated to form water by the cleavage of the O-O bond.
Similarly, MOF-818 catalyzes the oxidation of o-diphenols by
trinuclear copper centers in the presence of O and generates
rather than H O. Therefore, MOF-818 has good
2
2
have a similar mechanism by activating molecular O to yield
H
2
O
2
2
reactive oxygen species, which subsequently oxidize the
substrates and process the whole reactions. Accordingly, the
reported oxidase nanozymes usually exhibit low specificities
because they can catalyze the oxidation of a variety of
specificity and high catalytic activity as a novel catechol
oxidase nanozyme.
RESULTS AND DISCUSSION
reducing
substrates
including
ABTS,
TMB,
o-
MOF-818 was prepared by the reported method with some
modifications. MOF-818 is with trinuclear copper centers,
and TEM and SEM images revealed that most of the as-
phenylenediamine (OPD), ascorbic acid, ethanol, catechol, and
glutathione.
structural characteristics of natural enzymes is a feasible
strategy to improve the specificities of nanozymes.
40
32-36
Designing nanozymes by simulating the
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Figure 1. (a) Structure of MOF-818 and catechol oxidase (PDB: 1BT1). Color code: blue (N), white (C), red (O), turquoise (Cu). (b) TEM
images of MOF-818. (c) SEM images of MOF-818. (d) Cu 2p XPS spectrum of MOF-818. (e) Cu LMM Auger spectrum of MOF-818. (f)
Adsorption-desorption isotherm of nitrogen for MOF-818 at 77 K. (g) Experimental and simulated XRD patterns of MOF-818.
synthesized MOF-818 were octahedron in shape (Figure 1a-c).
The elemental composition and chemical bonding were
analyzed by X-ray photoelectron spectroscopy (XPS) (Figure
S1). The survey spectra of MOF-818 confirmed the presence
of C, O, N, Zr, and Cu, with atomic ratios of 74.66%, 23.47%,
activity. MOF-818 is stable in aqueous solution with various
pH values. The catechol oxidase-like activities of MOF-818
40
at different values of pH and temperature were measured. The
catalytic activity of MOF-818 gradually increased with
increasing pH value and temperature, and the rising trend
slowed down above pH 8 (Figure 2e-f). Therefore, PBS (pH
8.0) was used for further assays.
1
.32%, 0.23%, and 0.32%, respectively. Inductively coupled
plasma atomic emission spectroscopy (ICP-AES) was used to
identify the loadings of Cu (10.5 wt %) and Zr (11.9 wt %)
MOF-808, containing Zr ions only, was synthesized and
studied as the control. The TEM images revealed that most of
the as-synthesized MOF-808 samples were octahedrons in
shape and similar to that of MOF-818 (Figure S5). The crystal
structure of MOF-808 was characterized by XRD, which
matched well with the simulated XRD patterns (Figure S6). As
shown in Figure 3a, MOF-808 only had weak catechol oxidase
activity in contrast to MOF-818, indicating that Cu but not Zr
constructed the active center of MOF-818. Compared to the
absorption at 415 nm in the air-saturated buffer, the absorption
(
1
Table S1). The binding energy (BE) of Zr in MOF-818 was
82.5 eV, corresponding to the standard BE of Zr (Figure
4
+
S2). Cu 2p spectrum is shown in Figure 1d. The higher BE
2+
peak at 934.7eV was assigned to Cu , accompanied by the
2+
characteristic Cu shakeup satellite peaks (962.6 eV, 941.8
eV). The lower BE peak at 932.7 eV suggested the presence of
+
0
Cu and/or Cu species. Because Cu 2p3/2 XPS cannot
+
0
differentiate between Cu and Cu , Auger Cu LMM spectrum
was collected to confirm the presence of Cu at ~915 eV
+
(
Figure 1e). No peak was detected at 918-920 eV, indicating
0
that Cu was absent in MOF-818. Thus MOF-818 contained
Cu in the states of Cu and Cu . In Figure 1f, N adsorption-
2
+
2+
desorption isotherm of MOF-818 belonged to type IV
isotherm, as it was the typical mesoporous materials. The
multipoint BET surface area of MOF-818 was calculated to be
2
7
43.5 m /g. Pore size distributions for MOF-818 was analyzed
as shown in Figure S3. The crystal structure of MOF-818 was
characterized by XRD (Figure 1g). MOF-818 possessed an F-
centered cubic crystal lattice and matched well with the
4
0
simulated XRD pattern.
The oxidation process was monitored to study the catechol
oxidase-like activity of MOF-818 by using UV−vis
spectroscopy. As shown in Figure 2a, 3,5-DTBC had a strong
absorption at 278 nm and a new absorption peak appeared at
Figure 2. (a) UV-vis absorption spectra of 3,5-DTBC and 3,5-
DTBQ. (b) UV-vis absorption spectra over time in the presence of
0.5 mM 3,5-DTBC and 50 μg/mL MOF-818. (c, d) Time-
dependent absorbance at 415 nm with different concentrations of
MOF-818 in the presence of 0.5 mM 3,5-DTBC (c) and different
concentrations of 3,5-DTBC in the presence of 50 μg/mL MOF-
4
15 nm when it was oxidized to 3,5-di-tert-butyl-o-
benzoquinone (3,5-DTBQ). In the presence of MOF-818, the
absorption peak at 415 nm increased significantly over time
(Figure 2b). The absorption peak also increased with the
increasing concentration of MOF-818 and 3,5-DTBC,
indicating the evident enhancement of the reaction rate (Figure
2c-d). Similar phenomena were observed when L-dopa and
dopamine were used as the substrates (Figure S4),
demonstrating that MOF-818 possessed catechol oxidase-like
8
18 (d). Catechol oxidase-like activities of MOF-818 at different
pH values (e) and temperatures (f).
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of 3,5-DTBC catalyzed by MOF-818 showed a significant
increase in O -saturated condition and a decrease in N
peak still showed a strong signal that can be attributed to the
oxidation by Cu(II) (Figure 3b). On the other hand, the
reported oxidase nanozymes catalyze the oxidation by
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-
2
2
saturated condition. These suggested that oxygen was
necessary for this reaction (Figure 3b). To verify the
production during the reaction catalyzed by MOF-818,
horseradish peroxidase (HRP) and TMB were added to the
solution of MOF-818 and 3,5-DTBC (Figure 3c). When HRP
and TMB were both added to a mixed solution of MOF-818
and 3,5-DTBC, the characteristic absorption peak of oxidized
activating O
2
to yield reactive oxygen species, which
indistinguishably oxidize the substrates. Thus, they can
catalyze the oxidation of a variety of reducing substrates.
Oppositely, MOF-818 selectively catalyzes the oxidation of
3,5-DTBC but not TMB and ABTS, proving that the reaction
mechanism is completely different from the conventional
oxidase nanozyme reported.
2 2
TMB appeared at 650 nm, indicating that H O was generated
in the reaction. At the same time, due to the presence of
oxidized TMB, the absorption peak at 415 nm increased
significantly (Figure S7). However, when HRP and TMB were
added to a solution with either MOF-818 or 3,5-DTBC, the
absorption at 650 nm cannot be detected at all (Figure 3d). The
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presence of H
2
O
2
was further confirmed by Electron
Paramagnetic Resonance (EPR) in Figure 3e. Additionally,
EPR spectrum of Figure 3f proved the formation of o-
semiquinone radical in the system. Therefore, in this cascade
reaction, 3,5-DTBC is oxidized by O
formation of H , which further oxidizes TMB with the
catalysis of HRP. Further experimental results showed that
regardless of the presence of catalyst MOF-818 or not, H
had no substantial catalytic effect on the oxidation of 3,5-
DTBC (Figure S8), indicating that the effect of H on the
2
accompanied by the
2
O
2
2
O
2
2
O
2
catechol oxidase-like activity of MOF-818 is negligible under
the reaction conditions.
The catalytic effects of MOF-818 on different kinds of
substrates including TMB and ABTS were studied. Under
alkaline condition, the catalyst showed excellent catalytic
activity for 3,5-DTBC, but was unable to catalyze the
oxidation of TMB and ABTS (Figure S9). Under acidic
condition, MOF-818 can also slowly promote the oxidation of
3
,5-DTBC (Figure S10) without the ability to catalyze the
oxidation of TMB (Figure 4a). Moreover, CeO and Pt NPs
were synthesized to compare with MOF-818 in the catalysis
Figure S5). MOF-818 specifically catalyzed the oxidation of
3,5-DTBC without obvious peroxidase-like activity, while
CeO and Pt NPs can catalyze the oxidation of TMB and 3,5-
2
(
Figure 3. (a) UV-vis absorption spectra of 3,5-DTBC in the
absence and presence of 50 μg/mL MOF-818 or MOF-808. The
concentration of 3,5-DTBC was 0.5 mM. (b) The UV-vis
2
DTBC and exhibit both oxidase-like and peroxidase-like
activities (Figure 4a-d). Since the natural catechol oxidases do
not possess peroxidase activity, MOF-818 is the best candidate
as the nanozyme to mimic catechol oxidase among the
varieties of oxidase nanozyme. MOF-818 also showed higher
catalytic ability than that of previously reported catechol
absorption spectra of 3,5-DTBC in air-saturated, O
-saturated PBS solution (10 mM pH 8.0) with MOF-818. (c)
The scheme of detecting H . (d) UV-vis absorption spectra of
solutions with several combinations of MOF-818, 3,5-DTBC,
HRP and TMB (e) EPR spectrum of H in the reaction system.
f) EPR spectrum of o-semiquinone radical in the reaction system.
2
-saturated, and
N
2
2
O
2
2
O
2
2
nanozymes such as CeO and Pt NPs (Figure. 4c). Based on
(
the above results, MOF-818 with good specificity and high
catalytic activity had been certificated as a new catechol
oxidase nanozyme.
The oxidation rate of 3,5-DTBC was dependent on the
concentrations of both MOF-818 and the substrate. Increasing
the concentration of either MOF-818 or 3,5-DTBC resulted in
an evident enhancement of the reaction rate. The kinetic
studies of the oxidation of 3,5-DTBC were carried out by
monitoring the concentration of 3,5-DTBQ at 415 nm by
varying the concentration of 3,5-DTBC while keeping the
MOF-818 concentration constant. The reaction rate was found
to follow Michaelis–Menten kinetics. The Lineweaver–Burk
plot was calculated from the Michaelis–Menten curve (Figure
The possible reaction mechanism is proposed as illustrated
in Figure S11. 3,5-DTBC is oxidized to 3,5-DTBQ by
tricopper(II) centers to form the copper(I) species in a fast
reaction step. It is demonstrated that Cu(II) has the ability to
3
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oxidize a large number of organic compounds.
2
O is
necessary for the catalytic reaction and plays the role to
reoxidize copper(I) generated during the catalytic cycle while
H O is produced in a slow, rate-determining step. This
2 2
conjecture is well proved by the effect of oxygen
concentration on the reaction. The absorption peak at 415 nm
2
increased significantly in O -saturated condition compared to
the absorption in the air-saturated buffer, indicating that
oxygen engages the reaction as the oxidant. Although there
2
was a slight decrease in N -saturated buffer, the absorption
5
a-b). The enzyme kinetic constants K
and Kcat (catalytic constant) were obtained to measure the
enzyme efficiency. The calculated values for V , K
m
(Michaelis constant)
m
m
, Kcat and
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Figure 4. (a, b) UV-vis absorption spectra of the resultant solutions containing TMB and different catalysts in the absence (a) and presence
(
b) of H
different catalysts in phosphate buffer (10 mM pH 8.0). (d) Schematic illustration of the activity of MOF-818. (e) The nanozyme activities
of MOF-818, CeO , and Pt NPs. Insets: the color of solutions with the different substrates and nanozymes.
2 2
O in sodium acetate–acetic acid buffer solution (100 mM pH 4.0). (c) UV-vis absorption spectra of 3,5-DTBC in the presence of
2
K
4
cat/K
m
were 3.17 × 10 M s , 8.10 × 10 M, 0.383 s−1 and
-
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-4
To prove the universality of the catalyst, L-dopa and
dopamine were also selected as substrates to examine the
activity of the nanozyme. The catalyst showed significant
catalytic activities on both substrates. We measured the kinetic
constants of L-dopa. The Michaelis–Menten curve and
Lineweaver–Burk plot were obtained (Figure S15). The
2
-1 -1
.73 × 10 M s , respectively, indicating that MOF-818 has
excellent catalytic activity as a catechol oxidase mimic. As
shown in Figure S12 and Table S2, the enzyme kinetic
constants K and V of CeO and Pt NPs were accquired by
m m 2
using 3,5-DTBC as the substrate under the same conditions.
The results show that MOF-818 exhibits much higher catalytic
-8
m m m
calculated values for V , K , Kcat and Kcat/K were 7.97 × 10
-1
-4
−3
−1
-1
−1
efficiency than CeO
2
and Pt NPs.
M s , 4.8 × 10 M, 9.64 × 10 s , and 20.1 M s ,
respectively. Compared to 3,5-DTBC, L-dopa lead to a
dramatically decreased activity of MOF-818. It is assumed
that L-dopa is a relative stable chemical, and the complexation
of the amino group in L-dopa and copper in MOF-818 inhibits
the activity of the catalyst. As dopamine was used as the
substrate, MOF-818 could catalyze the oxidation of dopamine
to form polydopamine (Figure S4). Some other catechol
derivatives including quercetin, epicatechin and caffeic acid
were also oxidized with MOF-818 (Figure S16). Therefore,
MOF-818 is the catalyst for the oxidation of o-diphenols.
Table S2 compared the catalytic abilities of reported catechol
oxidase-like nanozymes and natural catechol oxidase.
To determine the product and calculate the yield, the UV-
vis spectra of a standard sample of 3,5-DTBQ and 3,5-DTBC
catalyzed by MOF-818 were collected (Figure S13a). The
results confirmed that the product of the oxidation was 3,5-
DTBQ. The standard curve of 3,5-DTBQ was measured
Figure S13b). According to the absorbance plateau reached
Figure S13c-d), 0.5 mM of 3,5-DTBC catalyzed by 30 μg/mL
of MOF-818 granted the yield of 98.2%.
(
(
The stability of MOF-818 has been tested by recycling
experiments and the reusable MOF-818 was characterized by
XRD. After four cycles in the HEPES buffer solution (10 mM
pH 8.0), MOF-818 still retained 70% of its activity. After five
cycles, there was no change in XRD data, indicating that
MOF-818 possesses excellent stability (Figure S14).
Phenolic compounds, such as chlorophenol, widely apply
for fungicides and preservatives and are common toxic
4
1
pollutants. These phenolic compounds pose a threat to
human health and are widely detected in soil and water, which
requires green catalysts for their degradations and detections.
It has been reported that potato polyphenol oxidase extracted
from commercial potatoes showed excellent catalytic activity
for the degradation of pentachlorophenol in the presence of
42
oxygen at room temperature. So the construction of a
nanozyme that mimics the natural enzyme to degrade and
detect chlorophenol is a promising strategy. To test the activity
of MOF-818, we used 2,4-dichlorophenol (2,4-DP) as the
substrate. The oxidation product of 2,4-DP reacted with 4-
aminoantipyrine (4-AAP) and generated a red product with an
absorbance at 510 nm, as shown in Figure S17. Thus, MOF-
818 has excellent catalytic activity as a nanozyme and shows
Figure 5. (a) Michaelis–Menten curves for 3,5-DTBC. (b)
Lineweaver-Burk plot for determination of kinetic constant of
MOF-818 for 3,5-DTBC. The concentration of MOF-818 was 50
μg/mL.
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good prospects in the detection and degradation of
chlorophenol.
(9) Natalio, F.; Andre, R.; Hartog, A. F.; Stoll, B.; Jochum, K. P.;
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Wever, R.; Tremel, W., Vanadium pentoxide nanoparticles mimic
vanadium haloperoxidases and thwart biofilm formation. Nat.
Nanotech. 2012, 7, 530-5.
CONCLUSIONS
In summary, we firstly proposed that MOF-818 has efficient
catechol oxidase-like activity with good specificity. MOF-818
can catalyze the oxidation of catechol to the corresponding o-
quinones but shows no peroxidase activity. The influence of
reaction conditions on the catalyst was systematically
investigated. Different from the previously reported catechol
oxidase nanozymes, MOF-818 catalyzed the oxidation of o-
(10) André, R.; Natálio, F.; Humanes, M.; Leppin, J.; Heinze, K.;
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2 2 2
diphenols and produced H O . In the present work, O was
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necessary and played the role to convert Cu(I) into Cu(II)
during the recycling. Moreover, by mimicking the active
center of natural catechol oxidase, MOF-818 exhibited
specificity and higher catalytic ability than that of the catechol
oxidase nanozymes previously reported.
(14) Wang, J.; Huang, R.; Qi, W.; Su, R.; Binks, B. P.; He, Z.,
Construction of a bioinspired laccase-mimicking nanozyme for the
degradation and detection of phenolic pollutants. Appl. Catal. B
Environ. 2019, 254, 452-462.
(15) Cheng, H.; Zhang, L.; He, J.; Guo, W.; Zhou, Z.; Zhang, X.;
Nie, S.; Wei, H., Integrated Nanozymes with Nanoscale Proximity for
in Vivo Neurochemical Monitoring in Living Brains. Anal. Chem.
ASSOCIATED CONTENT
The Supporting Information is available free of charge.
Experimental details, Figures S1−S17, Tables S1-S2, and
additional references.
2
016, 88, 5489-97.
16) Qin, L.; Wang, X.; Liu, Y.; Wei, H., 2D-Metal-Organic-
AUTHOR INFORMATION
Corresponding Author
(
Framework-Nanozyme Sensor Arrays for Probing Phosphates and
Their Enzymatic Hydrolysis. Anal. Chem. 2018, 90, 9983-9989.
*
dongsj@ciac.ac.cn, *fangyx@ciac.ac.cn.
(17) Wang, H.; Li, P.; Yu, D.; Zhang, Y.; Wang, Z.; Liu, C.; Qiu,
Author Contributions
H.; Liu, Z.; Ren, J.; Qu, X., Unraveling the Enzymatic Activity of
Oxygenated Carbon Nanotubes and Their Application in the
Treatment of Bacterial Infections. Nano Lett. 2018, 18, 3344-3351.
(18) Fan, K.; Xi, J.; Fan, L.; Wang, P.; Zhu, C.; Tang, Y.; Xu, X.;
Liang, M.; Jiang, B.; Yan, X.; Gao, L., In vivo guiding nitrogen-
doped carbon nanozyme for tumor catalytic therapy. Nat Commun
§
§
Minghua Li and Jinxing Chen contributed equally.
Notes
The authors declare no competing financial interest.
ACKNOWLEDGMENT
2
018, 9, 1440.
19) Luo, W.; Zhu, C.; Su, S.; Li, D.; He, Y.; Huang, Q.; Fan, C.,
(
This work is supported by the National Natural Science
Foundation of China (No. 21675151, 21705145 and 21721003)
and the Ministry of Science and Technology of China (No.
2016YFA0203203).
Self-Catalyzed, Self-Limiting Growth of Glucose Oxidase-Mimicking
Gold Nanoparticles. ACS Nano 2010, 4, 7451-7458.
(20) Komkova, M. A.; Karyakina, E. E.; Karyakin, A. A.,
Catalytically Synthesized Prussian Blue Nanoparticles Defeating
Natural Enzyme Peroxidase. J. Am. Chem. Soc. 2018, 140, 11302-
11307.
(21) Jiao, X.; Song, H.; Zhao, H.; Bai, W.; Zhang, L.; Lv, Y., Well-
redispersed ceria nanoparticles: Promising peroxidase mimetics for
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