DOI: 10.1002/slct.
201600575 Full Papers
z Inorganic Chemistry
An Oxido-Bridged Diiron(II) Complex as Functional Model
of Catechol Dioxygenase
Dhananjay Dey,[a] Abhranil De,[a] Hare Ram Yadav,[b] Partha Sarathi Guin,[c] Angshuman
Roy Choudhury,[b] Niranjan Kole,[a] and Bhaskar Biswas*[a]
This article is dedicated to Prof. Samir Kr. Chanda, Retired Associate Professor in Physics, Raghunathpur College, Purulia, West Bengal
An oxido-bridged diiron(II)-phenanthroline complex, [Fe2
O(phen)2Cl2] (1) [phen = 1,10-phenanthroline] has been synthe-
sized from an oxido-bridged diiron(III) precursor in presence of
sodium azide and structurally characterized by different spec-
troscopic tools including single crystal X-ray diffraction study.-
From X-ray crystal structure of 1, it is revealed that each of the
Fe(II) centre is in distorted octahedral geometry with FeN4OCl
core and the molecule crystallizes in Pnc2 space group. Bond
valence sum (BVS) calculation confirms the existence of iron
ions in + 2 oxidation state in 1. The diiron(II) complex has been
evaluated as model system for the catechol dioxygenase en-
zyme by using 3,5-di-tert-butylcatechol (DTBC) as the substrate
in acetonitrile medium, revealing that 1 efficiently mimics the
1. Introduction
In the active site of numerous metalloenzymes in biological
system, activation of kinetically inert molecular oxygen (O2) us-
ing redox properties of adjacent metal ions have received con-
siderable attraction to the bio-chemists. In view of the great
importance of oxidation reactions in industrial and synthetic
processes and of the ongoing search for new and efficient oxi-
dation catalysts, it is of paramount interest to elucidate the ba-
sic functional principles that govern such metallic reactivity of
natural enzymes.[1–3] From both environmental and economic
point of view, the search for effective catalytic oxidation proc-
esses that use clean, inexpensive terminal oxidants, such as
molecular oxygen or hydrogen peroxide is highly desired.[4]
[a] D. Dey, A. De, Dr. N. Kole, Dr. B. Biswas
Department of Chemistry, Raghunathpur College
Purulia 723 133,West Bengal, India
Fax: (+) 91 3251 255235
www.raghunathpurcollege.in
E-mail: icbbiswas@gmail.com
[b] H. R. Yadav, Dr. A. R. Choudhury
Department of Chemical Sciences,
Indian Institute of Science Education and Research Mohali,
S.A.S. Nagar, Manauli PO, Mohali 140 306, India
[c] Dr. P. S. Guin
Department of Chemistry,
Shibpur Dinobundhoo Institution (College)
Supporting information for this article is available on the WWW under
http://dx.doi.org/10.1002/slct.201600575
ChemistrySelect 2016, 1, 1910 – 1916
catalytic cycle of catechol dioxygenase. Upon stoichiometric
addition of DTBC pretreated with two equivalents of triethyl-
amine (Et3N) to the diiron complex, two catecholate-to-iron(III)
LMCT bands (515 nm and 734 nm) are observed. The in
situgenerated catecholate adduct from 1in acetonitrile solution
react with dioxygen to afford exclusively extradiol cleavage
products along with a small amount of benzoquinone, which is
also discerned from the appearance and decrease in intensity
of the electronic spectral bands around (708 nm; 507 nm) nm.
Nucleophilic attack by molecular oxygen on catecholate adduct
in solution provides substantial evidence for the regioselective
extradiol cleavage products.
The oxidative cleavage of catechol and other dihydroxy ar-
omatics is a key step in the biodegradation of naturally occur-
ring aromatic molecules and many aromatic environmental pol-
lutants by soil bacteria.[5, 6]Catechol dioxygenases are a class of
non-heme iron enzymes that catalyse the oxidative cleavage of
catechols. They are divided into two subclasses: the intradiol di-
oxygenases, which utilize a non-heme iron(III) cofactor in cata-
lyzing the cleavage of the carbon–carbon bond between the
two catechol oxygens; and the extradiol dioxygenases, which
utilize a nonheme iron(II) cofactor in catalyzing the cleavage of
the carbon–carbon bond adjacent to the catechol oxygen-
s.[7, 8]The study of mixed-valent iron complexes of ligands with
phenolate oxygen and pyridine nitrogen donorshave provided
valuable information to elucidate the structure–function corre-
lation for the active site geometries of the catechol dioxyge-
nase enzymes.[9–11]With the aim to develop more active catalytic
systems and to gain new insight in the enzymatic mechanism,
we have designed, synthesized and structurally characterized a
diiron(II) complex in solid state using reducing properties of so-
dium azide at refluxing condition.From Bond Valence Sum cal-
culation it is revealed that iron centres are in + 2 oxidation
state in the solid state.We have also explored the catechol diox-
ygenase activity of the diiron(II) complex towards molecular
oxygen in acetonitrile medium which revealed superior se-
lectivity towards extradiol cleavage products and suggests sub-
strate activation mechanism for the oxidative extradiol cleav-
age of catechols
1910  2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
 Full Papers
2. Results and Discussion ture. The molecular structure of the complex is illustrated in
Figure 1. The two iron(II) centres of the dinuclear iron(II) com-
2.1. Synthesis and formulation
The oxido-bridged dinuclear iron(II)-phenanthroline complex
was synthesized and isolated in crystalline phase from an ox-
ido-bridged diiron(III) precursor, tetraethylammonium[(m-oxi-
do)bis[trichloroferrate(III)], (Et4N)2[Fe2OCl6]by mixing sodium
azide, (NaN3) and 1,10-phenanthroline in an aqueous medium
under refluxing condition. The coordination geometry of 1was
determined by single crystal X-ray diffraction study along with
different spectroscopic and analytical techniques.

2.2. Proposed mechanistic pathway for the formation of 1

To investigate the mechanistic pathway behind the formation
of oxido-bridged diiron(II) complex as major product, we ob-
served that NaN3 helped to create reducing environment in the
reaction mixture.[12] At the primary stage of the reaction the yel-
low solution of the precursor turned instantly brown during
the addition of azide and indicated the incorporation of the
azide ions into the coordination sphere of iron centres with the
displacement of chloride ions.At refluxing condition, in acidic
medium, Fe(III) centres reduced to Fe(II) ions which were well
stabilized by the addition of 1,10-phenanthroline (p-acidic li-
gand), knownasgood stabilizer[13] for metal ions having lower
oxidation states. The chloride salts were separated and purified
from the reaction mixture using diethyl ether-water as eluant
mixture. The separated and isolated molecular salt, Et4NCl was
also characterized by IR, UV-Vis and 1H NMR spectroscopy. Con-
trolled experiments under the same conditions in the absence
of NaN3 revealed that for successful production of this oxido-
bridged diiron(II)-phen complex, sodium azide ion is essential
(Scheme 1).
Figure 1. An ORTEP diagram of diiron(II) complex (1) with atom numbering
scheme and 30 % probability ellipsoids.
plex are bridged by the O(3) atom and each of the Fe(II) ion are
surrounded by two phenanthrolinemolecules, one chlorine and
one oxido-linkage in a distorted octahedral geometry (Fig-
ure 1).Two phenanthroline molecules coordinate to each of the
Fe(II) ion, with Fe–N distances of 2.141(4) , 2.212(4) , 2.227(4)
 and 2.112(4)  for Fe(1)–N(2), Fe(1)–N(5), Fe(1)–N(10), and
Fe(1)–N(40), respectively. The Fe–O–Fe linkage is nonlinear, ex-
hibiting an angle of 165.06(4)8 for Fe(1)–O(3)–Fe(1). The Fe–m-
O(3) distance [1.784(12) ] is in accordance with those pre-
viously reported for (FeL)2O (1.76–1.82 ).[14] The combination
of the nonlinear bridge and the strong Fe(II)–m-O(3) bonding
produces an intermetallic spacing of 3.538 . The bond lengths
of C–N and C–C in the phenanthroline all fall within the range
of the literature values[15] and the two aromatic ring systems in
each phen are coplanar within the experimental error.
Investigation on the supramolecular assembly of the neu-
tral diiron(II) complex shows that diiron(II) unitsare associated
with neighbouring unit through strong C H···Cl hydrogen-
bonding interactions along the crystallographic b axis which
also leads to the formation of a 1D chain (Figure 2) (C7-
H7···Cl1 = 2.945 ).

Scheme 1. Proposed mechanistic pathway for the formation of 1.

2.3. Description of crystal structure

Single crystal X-ray diffraction analysis reveals that 1 crystallizes
Figure 2. Supramolecular construction of 1D chain via H7···Cl1 interaction
in the orthorhombic unit cell with space group Pnc2. The asym-
(green dotted bond) along b-axis.
metric unit contains half of the molecule with the 2 fold axis
passing through the O atom linking between the two Fe
atoms. Therefore the value of Z’ is 0.5 and Z = 2 for this struc-

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Table 1. Crystal data and structure refinement parameters for 1.

tral bands at 225, 266, 326 and 522 nm appeared in the elec-
tronic spectrum of 1in acetonitrile, whereas DTBC showed a
Parameters 1
single band at 284 nm. Upon adding DTBC to the iron(II) com-
Empirical formula C48H32N8Cl2OFe2 plex, there was a gradual decrease in intensity of the band due
Formula weight 973.42 to the catechol at 284 nm[17] and an initial new band was
Temperature (K) 296
formed at ~ 406 nm (Figure 3) indicating the rapid formation of
Crystal system Orthorhombic
Space group Pnc2
a () 13.813(3)
b () 18.120(3)
c () 10.497(19)
Volume (3) 2627.4(9)
Z, Z’ 2, 1
1 (gcm–3) 1.162
m (mm–1) 0.693
F (000) 940
q ranges (8) 3.2-27.5
Rint 0.098
R (reflections) 23233
wR2 (reflections) 5995
Final R indices 0.0626, 0.1867
Largest peak and hole (e 3) 0.41, 0.31

2.4. Bond Valence Sum (BVS) calculation

Figure 3. UV-vis spectral change of iron complex at a regular interval of

Bond Valence Sum (BVS)[16] an empirical quantity, has been
5 min with 3,5-DTBC.
used to determine the oxidation state of each of the Fe centres
in 1in solids from the crystallographically determined bond dis-
tance data. Bond valence (S) = exp.[(R0-Rij)/B], Oxidation state =
Sbond valences; Rij is the observed bond length, the usual pro- DTBQ in solution.[17] Interestingly, at the same time an intense
cedure is to assume an oxidation state and to use previously catecholate-to-iron(III) LMCT band ~ 734 nm[18] with gradual in-
determined R0 values appropriate to the bond being consid- crease in intensity (Figure 4) and a Fe(II)-semiquinone band[18]
ered. The constant B is determined as 0.37. If in the present
complex, Fe centres are assumed to have + II oxidation state,
then R0 values for Fe O and Fe N are taken as 1.734 and
1.806 , respectively. Since, the diiron(II) complex is a cen-
trosymmetric molecule, hence the BVS found for each of the
iron centres is 1.88.
If in the present complex, Fe ions are considered to have +
III oxidation state then R0 for Fe O and Fe N are 1.759 and
1.855 , respectively. Thus, the BVS found for each of the iron
centres is 2.08. So, from the BVS study it can be further con-
cluded that the oxidation state for both the iron ions in 1is + 2.

2.5. Spectrophotometric investigation for the formation of

in situ iron–catecholate adduct
In order to investigate the catechol dioxygenase reactivity, ini-
tially we studied the efficiency of formation of iron-catecholate
adduct by taking 1with 3,5-di-tert-butylcatechol (DTBC) in oxy-
gen saturated acetonitrile at 25 8C. The formation of the en-
zyme-substrate adduct at transition state remains the most fun-
damental aspects for the conversion of substrate to product in
catalytic oxidation reactions, and to determine catalytic effi-
ciency of the metal complex. For this purpose, a catalytic
amount of this diiron(II) complex (1 3 10 4 M) solution was
treated with 1 3 10 2 M of DTBC in acetonitrile medium and
the course of the reaction was followed by recording the UV–-
Vis spectra of the mixture at an interval of 5 min for 2 h. Spec-
Figure 4. In situ formation of Fe(III)-catecholate adduct at 734 nm (The spec-
tra were recorded after every 5 min).
which gradually decrease in intensity ~ 515 nm(Figure 3) was
observed for 1. Electronspray ionization (ESI) mass spectral
analysis (Figure S1) of the reaction mixture further revealed
that, effective formation of the Fe(III)-catecholate adduct, {[Fe(-
phen)2(DTBC)]H + } at m/z 636.47 and [Na(DTBQ)] + at m/z 243.09
in ACN solution is observed. The effective in situ generation of

ChemistrySelect 2016, 1, 1910 – 1916 1912  2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim

the Fe(III)-catecholate adduct is also concerned from EPR spec-
tral analysis of the mixture. Though the EPR spectrum of the
frozen solution of diiron(II) complex in acetonitrile medium re-
mains silent (Figure S2) but upon addition of the DTBC in 1dis-
play high-spin (S = 5/2) rhombic ferric signals[19, 20]at g = 7.79,
4.33, 2.10 (Figure S2).
2.6. Reactivity of in situ Fe(III)-catecholate complex toward
dioxygen
The reactivity of the in situ Fe(III)-catecholate adduct toward di-
oxygen was investigated to determine the catechol cleavage
products. The red solution of 1 reacts with dioxygen in acetoni-
trile at ambient conditions over a period of 6 h to give a green
solution. During the reaction, the catecholate-to-iron(III) adduct
is found to react as observed from the decrease in absorbance
of the catecholate-to-iron(III) LMCT band at ~ 708 and
507 nm(Figure 5). The disappearance of the lower-energy cat-
Figure 5. Absorption spectral changes during the reaction of the in
situgenerated adduct [Fe(phen)2(DBC)] + with O2 (The spectra were recorded
after every 9 min). Inset: plot of absorbance versus time exhibiting cleavage
of catecholate adduct.
echolate-to-iron(III) LMCT band (Figure 5) on oxygenation ex-
hibits pseudo first-order kinetics, as judged from the linearity of
the plot [1 + log(Absorbance)] versus time[21, 22](Figure 6), and
the value of kobs was obtained from the slope of the plot. The
pseudo-first order rate constant was determined as kobs: 9.89 3
10 4 min 1.
The rate of disappearance of this LMCT band for this Fe(III)-
catecholate adduct is slower than the rate for the complexes
reported by Paine et al, Que et al and Palanadivar et al.[7].This
result indicates that isolated Fe-catecholate complex reacts
more effectively with dioxygen compared to in situ formed cat-
echolate adducts. Further, the oxidized products from catechol
bound Fe(III) species were identified and quantified by 1H NMR
spectroscopy (Figure S3), ESI-MS (Figure S4) and HPLC (Figure
S5). The distribution of catechol-derived products was found
mainly 4,6- di-tert-butyl-2-pyrone, 3,5- di-tert-butyl-2-pyrone, as
extradiol cleavage products in quantitative yield along with the
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Figure 6. Plots of [1 + log(Absorbance)] versus time for the reaction of
[Fe(L)(DBC)(Sol)] + with O2 at 25 8C in MeCN solution.
formation of little 3,5-di-tert-butylbenzoquinone. In the reaction
of (1 + DTBC) with O2 in acetonitrile, 71 % (51.5 + 19.5) of extra-
diol cleavage products were obtained along with the formation
of small amount of intradiol cleavage products (3.7 % + 2.0 %)
as side products. The percentage of another oxidation product,
3,5-di-tert-butylbenzoquinone, was found to be a small one
(7.5 %) also. The amount of organic product from catechol
cleavage accounts for 84.2 % of 3,5-di-tert-butyl catechol. The
remaining 15.8 % was accounted as unreacted substrate. In
contrast, in the work of Klein Gebbink et al.[23] and M. Pala-
niandivar et al.[24] with a model iron-catecholate complex of a
facial N,N,O donor ligand, the major product was the quinone.
Therefore, the diiron(II) complex reported here is an addition to
the reported catecholate complexes supported by N,N,O donor
ligands.
2.7. Electrochemical behavior of Fe(III)-DTBC adduct
Electrochemical analysis of 1 and (1 + 3,5-DTBC) under oxygen
atmosphere in anhydrous dimethylsulfoxide medium (DMSO) in
the presence of tetrabutylammonium bromide as supporting
electrolyte was studied using cyclic voltammetry. In DMSO, the
diiron(II) complex probably partially decomposes into a mono-
iron species which are also reflected from three successive irre-
versible one-electron reductions showing three peaks
at 1.25, 1.42 and 1.68 V vs. Ag/AgCl, saturated KCl (Figure 7,
Curve 1). Chronocoulometry studies at constant potential es-
tablished that in each reduction, only one electron is involved.
The cyclic voltammetry of background solution (Figure S6)
showed that there is no oxidation or reduction peak, clearly
suggesting the fact that three reduction peaks observed in the
cyclic voltammogram of 1 was exclusively due to the reduction
of iron species. The Earlier studies on the electrochemical be-
havior of iron complexes[24] also showed that one electron re-
duces the central Fe(III) to Fe(II), thereby producing one reduc-
tion peak. The irreversibility of these reduction may be due to
greater stability of Fe(II) in the coordination environment of
phenanthroline in the three iron species [two iron centres of
diiron(II) complex, and mononuclear iron species with DMSO].
A plot of cathodic peak current (Ipc) versus the square root of
1913  2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim

Figure 7. Cyclic voltammogram of 0.1 mM Fe complex in the absence (Curve
1) and presence (Curve 2) of 3,5-DTBC and cyclic voltammogram of 3,5-DTBC
(Curve 3) at the glassy carbon electrode surface in DMSO media. Scan rate:
0.050 Vs 1. [TBAB] = 0.1 M, T = 298.15 K.
scan rate (v1/2) for the three reductions showed linear relation-
ship (Figure 8) which means that the reductions are fully dif-
Figure 8. Plot of cathodic peak currents (Ipc) of the reversible peak (I) vs. the
square root of the scan rates (v1/2) for the reduction of the iron complex at
the glassy carbon electrode surface in DMSO media; * = 1st reduction,
* = 2nd reduction, D = 3rd reduction.
fusion controlled and there is no adsorption of the species at
the electrode surface during the course of electrochemical re-
duction.
Under controlled experimental conditions the cyclic voltam-
mogram of 3,5-DTBC in the absence of 1, (Figure 7, Curve 3)
shows no significant reduction or oxidation peak. The cyclic
voltammogram of the mixture of 1and 3,5-DTBC (Figure 7,
Curve 2) shows two quasireversible reduction peaks at + 0.18
ChemistrySelect 2016, 1, 1910 – 1916
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and - 0.19 V along with three irreversible reduction peaks
at 1.18, 1.42 and 1.68 V. Comparing the cyclic voltammo-
grams of 1 in the absence (Figure 7, Curve 1) and in the pres-
ence of 3,5-DTBC (Figure 7, Curve 2) it may be said that three
irreversible reduction peaks of 1and 3,5-DTBC in mixture is ex-
clusively due to the reduction of three different Fe(III) species.
A Comparison of the cyclic voltammograms of 3,5-DTBC in the
absence and presence of 1 (Curve 2 and 3, Figure 7) shows that
two quasireversible reduction peaks at + 0.18, - 0.19 V (Fig-
ure 7, Curve 2) is due to generation of a (The sentences should
be in one paragraph)
oxidized product of the hydroquinone, i. e. 3,5-DTBC. A lot
of earlier studies on the electrochemical behavior of various
quinones in organic polar media such as DMSO, DMF, acetoni-
trile, etc. showed that quinones undergo quasireversible or re-
versible two step one-electron reductions generating semi-
quinone and quinone dianion thereby generating two
quasireversible or reversible reduction peaks.[25, 26] Comparing
the electrochemical properties of 3,5-DTBC in the presence of
iron complex with that of the earlier[25, 26], it can be concluded
that in the present study two quasireversible reduction peaks
at + 0.18 and - 0.19 V are solely due the generation of semi-
quinone and quinone dianion by the oxidation of 3,5-DTBC by
the iron complex in the reaction media. Thus Fe(III) species cat-
alyzes the oxidation of 3,5-DTBC in solution and it is reduced to
Fe(II). The generation of Fe(II) in the catalytic pathways was
confirmed by the appearance of an oxidation peak at 1.8 V
(Curve 2, Figure 7).
2.8. Reactivity and reaction mechanism
The [FeIII(phen)DTBC] complexes react with dioxygen to yield
products due to the oxidative cleavage of the catechol ring.-
Several groups of scientists provided valuable information re-
garding catalytic cycles in favour of the production of cleavage
and oxidation products. Bugg and co-workers[27] have ruled out
the formation of the dioxetane intermediate proposed in the
molecular oxygen activation (extradiol cleavage) as well as in
the substrate activation (intradiol cleavage) mechanisms and
proposed that cyclohexadienyl peroxide is the common inter-
mediate formed in both of these mechanisms. L. Que etal. had
proposed[28, 29] that the increased Lewis acidity of the ferric cen-
ter enhances the covalency of the metal-catecholate interaction
and the semiquinone character of the bound catecholate,
thereby activating the catecholate for reaction with O2.[28] Fur-
ther, when dioxygen attacks the activated carbon atom of cat-
echolate substrate strongly bound to the iron(III) center in the
adduct (substrate-activation mechanism), the Criegee inter-
mediate [(L)(DBSQ)Fe(III)O2] gives intradiol cleavage products
upon acyl migration and extradiol cleavage products upon al-
kenyl migration.[29, 30]Studies with enzymes and models have
also established that both iron(II) and iron(III) can catalyze the
extradiol cleavage of catechol.[31, 32]The key to originate quanti-
tative extradiol cleavage products from oxygen activation on
iron-catecholate adduct or Fe-DTBC complex lies in the avail-
ability of a coordination site around the metal centre. While in-
tradiol cleavage must involve the direct attack of an electro-
1914  2016 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
 Full Papers
philic O2 molecule on the enediolate moiety of the coordinated
catecholate adduct, in extradiol cleavage the initial C O bond-
forming step must occur at the carbon adjacent to the enedio-
late moiety. This distinct regiochemistry can only be achieved
by a different mode of attack, which L. Que etal. proposed that
of a nucleophilic superoxide on an electrophilic site on the ar-
omatic ring.[33] The availability of an iron coordination site al-
lows O2, to bind to the iron center, thereby forming an FeII-su-
peroxide complex. Here, the experimental observations
correlates well with scientific literature and provide the under-
lying rationale for the substrate activation mechanism. This is
probably due to the availability of a labile coordination site on
the Fe(III) center that allows the substrate to bind with iron
center and produce Fe(II)-semiquinone which facilitates the co-
ordination of dioxygen. The conversion of the semiquinone
into a monodentate ligand brings the bound superoxide in
close proximity to a ring carbon adjacent to the enediol unit.
The nucleophilic superoxide can then attack the ring at this
carbon to effect a Michael addition on the dienone function;
Scheme 2. Proposed mechanistic pathway for the formation of cleavage
subsequent decomposition of the resultant peroxide affords products by 1.
the observed pyrone products. The regiospecificity of oxidative
cleavage is thus determined by the nature of the dioxygen spe-
cies that attacks the bound catechol: nucleophilic attack by su-
peroxide for extradiol cleavage versus electrophilic attack by pound breaks down into mononuclear Fe(III) species. The diir-
O2, for intradiol cleavage.[34]At present, the first mechanism on(II) complex has been evaluated as model system for the
plays the crucial role in favour of the production of extradiol catechol dioxygenase enzyme by using 3,5-di-tert-butylcatechol
products as 4,6-di-tert-butyl-2-pyrone or 3,5-di-tert-butyl-2-py- (DTBC) as the substrate in acetonitrile medium, revealing that 1
rone and 3,5-di-tert-butyl-quinone as major products. The facial efficiently mimics the catalytic cycle of catechol dioxygenase
coordination of the supporting ligand further allows in forming exzyme and exclusively Experimental Section
a peroxo intermediate to adopt a pseudo-axial arrangement at
iron centre. The heterolytic O–O bond cleavage involved in
Supporting Information
Criegee rearrangement is assisted by the presence of a proton
affording the extradiol cleavage product. The ESI-MS data of CCDC 1428629 contains the supplementary crystallographic
the catechol cleavage products (Figure S4) after separation of data for 1. These data can be obtained free of charge via
the reaction mixture also provides fundamental in- http://www.ccdc.cam.ac.uk/conts/retrieving.html or from the
formation.The mass spectrum of the cleavage products exhibits Cambridge Crystallographic Data Centre, 12 Union Road, Cam-
mainly the characteristics peaks at m/z 209.25, 243.27 and bridge CB2 1EZ, UK; fax: (+ 44) 1223–336-033; or e-mail: depos-
295.40 with isotope distribution patterns which further con- it@ccdc.cam.ac.uk. Experimental information such as UV-Vis and
solidated the corroboration respectively [(4,6-di-tert-butyl-2- py- infrared spectrum of 1, ESI mass spectra, 1H NMR of catechol
rone) + H + ] or [(3,5-di-tert-butyl-2-pyrone) + H + ], [Na(DTBQ)] + cleavage products,HPLC plot, cyclic voltagram of TBAB, and
and [K(3,5-di-tert-butyl-5-(carboxymethyl)-2-furanone)] + . Also, bond distance, bond angle parameters are given here.
the simultaneous production of hydrogen peroxide during the
catechol dioxygenase activity by in situ formed catecholate ad-
Acknowledgements
duct follows the catalytic cycle as shown in Scheme 2.
DD thanks the Science & Engineering Research Board (SERB),
New Delhi for his fellowship. The work is supported financially
3. Conclusions
by SERB India under the FAST TRACK SCHEME for YOUNG SCI-
The m-oxido-bridged diiron(II) complex containing the phenan- ENTIST (No. SB/FT/CS-088/2013 dtd. 21/05/2014). HRY gratefully
throline ligand wasdesigned andsynthesized from a m-oxido- acknowledges the research fellowship received from UGC, India
bridged diiron(III) precursor using the reducing property of so- through UGC-NET JRF programme. ARC thanks the X-ray facility
dium azide in a novel synthetic route. Controlled experiments of the Department of Chemical Sciences, IISER Mohali for single
under the same conditions in the absence of NaN3 can’t suc- crystal X-ray diffraction data collection.
cessfully produce this oxido-bridged diiron(II)-phen complex.
The diiron(II) complex was structurally characterized by differ- Keywords: Iron · Synthesis · X-ray structure · Catechol
ent spectroscopic tools including single crystal X-ray diffraction Dioxygenase activity
study. Though the dinuclear iron(II) complex is stable in aceto-
nitrileic medium but upon addition of DTBC, the diiron(II) com-

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Submitted: May 20, 2016
Accepted: May 25, 2016
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