Accessing a synthetic FeIIIMnIV core to model biological heterobimetallic active sites.

Metalloproteins with dinuclear cores are known to bind and activate dioxygen, with a subclass of these proteins having active sites containing FeMn cofactors and activities ranging from long-range proton-coupled electron transfer (PCET) to post-translational peptide modification. While mechanistic studies propose that these metallocofactors access FeIIIMnIV intermediates, there is a dearth of related synthetic analogs. Herein, the first well-characterized synthetic FeIII-(µ-O)-MnIV complex is reported; this complex shows similar spectroscopic features as the catalytically competent FeIIIMnIV intermediate X found in Class Ic ribonucleotide reductase and demonstrates PCET function towards phenolic substrates. This complex is prepared from the oxidation of the isolable FeIII-(µ-O)-MnIII species, whose stepwise assembly is facilitated by a tripodal ligand containing phosphinic amido groups. Structural and spectroscopic studies found proton movement involving the FeIIIMnIII core, whereby the initial bridging hydroxido ligand is converted to an oxido ligand with concomitant protonation of one phosphinic amido group. This series of FeMn complexes allowed us to address factors that may dictate the preference of an active site for a heterobimetallic cofactor over one that is homobimetallic: comparisons of the redox properties of our FeMn complexes with those of the di-Fe analogs suggested that the relative thermodynamic ease of accessing an FeIIIMnIV core can play an important role in determining the metal ion composition when the key catalytic steps do not require an overly potent oxidant. Moreover, these complexes allowed us to demonstrate the effect of the hyperfine interaction from non-Fe nuclei on 57Fe Mössbauer spectra which is relevant to MnFe intermediates in proteins.

Modulation of the Bonding between Copper and a Redox-Active Ligand by Hydrogen Bonds and Its Effect on Electronic Coupling and Spin States.

The exchange coupling of electron spins can strongly influence the properties of chemical species. The regulation of this type of electronic coupling has been explored within complexes that have multiple metal ions but to a lesser extent in complexes that pair a redox-active ligand with a single metal ion. To bridge this gap, we investigated the interplay among the structural and magnetic properties of mononuclear Cu complexes and exchange coupling between a Cu center and a redox-active ligand over three oxidation states. The computational analysis of the structural properties established a relationship between the complexes' magnetic properties and a bonding interaction involving a dx2-y2 orbital of the Cu ion and π orbital of the redox-active ligand that are close in energy. The additional bonding interaction affects the geometry around the Cu center and was found to be influenced by intramolecular H-bonds introduced by the external ligands. The ability to synthetically tune the d-π interactions using H-bonds illustrates a new type of control over the structural and magnetic properties of metal complexes.

Influence of the ligand-field on EPR parameters of cis- and trans-isomers in MoV systems relevant to molybdenum enzymes: Experimental and density functional theory study.

The electron paramagnetic resonance (EPR) investigation of mononuclear cis- and trans-(L1O)MoOCl2 complexes [L1OH = bis(3,5-dimethylpyrazolyl)-3-tert-butyl-2-hydroxy-5-methylphenyl)methane] reveals a significant difference in their spin Hamiltonian parameters which reflect different equatorial and axial ligand fields created by the heteroscorpionate donor atoms. Density functional theory (DFT) was used to calculate the values of principal components and relative orientations of the g and A tensors, and the molecular framework in four pairs of isomeric mononuclear oxo­molybdenum(V) complexes (cis- and trans-(L1O)MoOCl2, cis,cis- and cis,trans-(L-N2S2)MoOCl [L-N2S2H2 = N,N'-dimethyl-N,N'-bis(mercaptophenyl)ethylenediamine], cis,cis- and cis,trans-(L-N2S2)MoO(SCN), and cis- and trans-[(dt)2MoO(OMe)]2- [dtH2 = 2,3-dimercapto-2-butene]). Scalar relativistic DFT calculations were conducted using three different exchange-correlation functionals. It was found that the use of hybrid exchange-correlation functional with 25% of the Hartree-Fock exchange leads to the best quantitative agreement between theory and experiment. A simplified ligand-field approach was used to analyze the influence of the ligand fields in all cis- and trans-isomers on energies and contributions of molybdenum d-orbital manifold to g and A tensors and relative orientations. Specifically, contributions that originated from the spin-orbit coupling of the dxz, dyz, and dx2-y2 orbitals into the ground state have been discussed. The new findings are discussed in the context of the experimental data of mononuclear molybdoenzyme, DMSO reductase.

The Mechanism of Formation of Active Fe-TAMLs Using HClO Enlightens Design for Maximizing Catalytic Activity at Environmentally Optimal, Circumneutral pH.

Fe-TAML/peroxide catalysis provides simple, powerful, ultradilute approaches for removing micropollutants from water. The typically rate-determining interactions of H2O2 with Fe-TAMLs (rate constant kI) are sharply pH-sensitive with rate maxima in the pH 9-10 window. Fe-TAML design or process design that shifts the maximum rates to the pH 6-8 window of most wastewaters would make micropollutant eliminations even more powerful. Here, we show how the different pH dependencies of the interactions of Fe-TAMLs with peroxide or hypochlorite to form active Fe-TAMLs (kI step) illuminate why moving from H2O2 (pKa, ca. 11.6) to hypochlorite (pKa, 7.5) shifts the pH of the fastest catalysis to as low as 8.2. At pH 7, hypochlorite catalysis is 100-1000 times faster than H2O2 catalysis. The pH of maximum catalytic activity is also moderated by the pKa's of the Fe-TAML axial water ligands, 8.8, 9.3, and 10.3, respectively, for [Fe{4-NO2C6H3-1,2-(NCOCMe2NSO2)2CHMe}(H2O)n]- (2) [n = 1-2], [Fe{4-NO2C6H3-1,2-(NCOCMe2NCO)2CF2}(H2O)n]- (1b), and [Fe{C6H4-1,2-(NCOCMe2NCO)2CMe2}(H2O)n]- (1a). The new bis(sulfonamido)-bis(carbonamido)-ligated 2 exhibits the lowest pKa and delivers the largest hypochlorite over peroxide catalytic rate advantage. The fast Fe-TAML/hypochlorite catalysis is accompanied by slow noncatalytic oxidations of Orange II.

A 4H+/4e- Electron-Coupled-Proton Buffer Based on a Mononuclear Cu Complex.

In this research article, we describe a 4H+/4e- electron-coupled-proton buffer (ECPB) based on Cu and a redox-active ligand. The protonated/reduced ECPB (complex 1: [Cu(8H+/14e-)]1+), consisting of CuI with 2 equiv of the ligand (catLH4: 1,1'-(4,5-dimethoxy-1,2-phenylene)bis(3-(tert-butyl)urea)), reacted with H+/e- acceptors such as O2 to generate the deprotonated/oxidized ECPB. The resulting compound, (complex 5: [Cu(4H+/10e-)]1+), was characterized by X-ray diffraction analysis, nuclear magnetic resonance (1H-NMR), and density functional theory, and it is electronically described as a cuprous bis(benzoquinonediimine) species. The stoichiometric 4H+/4e- reduction of 5 was carried out with H+/e- donors to generate 1 (CuI and 2 equiv of catLH4) and the corresponding oxidation products. The 1/5 ECPB system catalyzed the 4H+/4e- reduction of O2 to H2O and the dehydrogenation of organic substrates in a decoupled (oxidations and reductions are separated in time and space) and a coupled fashion (oxidations and reductions coincide in time and space). Mechanistic analysis revealed that upon reductive protonation of 5 and oxidative deprotonation of 1, fast disproportionation reactions regenerate complexes 5 and 1 in a stoichiometric fashion to maintain the ECPB equilibrium.

Bioinspired Di-Fe Complexes: Correlating Structure and Proton Transfer over Four Oxidation States.

Metalloproteins with active sites containing di-Fe cores exhibit diverse chemical reactivity that is linked to the precise transfer of protons and electrons which directly involve the di-Fe units. The redox conversions are commonly corroborated by spectroscopic methods, but the associated structural changes are often difficult to assess, particularly those related to proton movements. This report describes the development of di-Fe complexes in which the movements of protons and electrons are pinpointed during the stepwise oxidation of a di-FeII species to one with an FeIIIFeIV core. Complex formation was promoted using the phosphinic amido tripodal ligand [poat]3- (N,N',N″-[nitrilotris(ethane-2,1-diyl)]tris(P,P-diphenylphosphinic amido)) that provided dynamic coordination spheres that assisted in regulating both electron and proton transfer processes. Oxidation of an [FeII-(µ-OH)-FeIII] complex led to the corresponding di-FeIII species containing a hydroxido bridge that was not stable at room temperature and converted to a species containing an oxido bridging ligand and protonation of one phosphinic amido group to form [Hpoat]2-. Deprotonation led to a new species with an [FeIII-(µ-O)-FeIII] core that could be further oxidized to its FeIIIFeIV analogue. Reactions with phenols suggest homolytic cleavage of the O-H bond to give products that are consistent with the initial formation of a phenoxyl radical─spectroscopic studies indicated that the electron is transferred to the FeIV center, and the proton is initially transferred to the more sterically hindered oxido ligand but then relocates to [poat]3-. These findings offer new mechanistic insights related to the stability of and the reactions performed by di-Fe enzymes.

Stepwise assembly of heterobimetallic complexes: synthesis, structure, and physical properties.

Bimetallic active sites are ubiquitous in metalloenzymes and have sparked investigations of synthetic models to aid in the establishment of structure-function relationship. We previously reported a series of discrete bimetallic complexes with [FeIII-(µ-OH)-MII] cores in which the ligand framework provides distinct binding sites for two metal centers. The formation of these complexes relied on a stepwise synthetic approach in which an FeIII-OH complex containing a sulfonamido tripodal ligand served as a synthon that promoted assembly. We have utilized this approach in the present study to produce a new series of bimetallic complexes with [FeIII-(µ-OH)-MII] cores (M = Ni, Cu, Zn) by using an ancillary ligand to the FeIII center that contains phosphinic amido groups. Assembly began with formation of an FeIII-OH that was subsequently used to bind the MII fragment that contained a triazacyclononane ligand. The series of bimetallic complexes were charactered structurally by X-ray diffraction methods, spectroscopically by absorption, vibrational, electron paramagnetic resonance spectroscopies, and electrochemically by cyclic voltammetry. A notable finding is that these new [FeIII-(µ-OH)-MII] complexes displayed significantly lower reduction potentials than their sulfonamido counterparts, which paves way for future studies on high valent bimetallic complexes in this scaffold.

Artificial Metalloproteins with Dinuclear Iron-Hydroxido Centers.

Dinuclear iron centers with a bridging hydroxido or oxido ligand form active sites within a variety of metalloproteins. A key feature of these sites is the ability of the protein to control the structures around the Fe centers, which leads to entatic states that are essential for function. To simulate this controlled environment, artificial proteins have been engineered using biotin-streptavidin (Sav) technology in which Fe complexes from adjacent subunits can assemble to form [FeIII-(µ-OH)-FeIII] cores. The assembly process is promoted by the site-specific localization of the Fe complexes within a subunit through the designed mutation of a tyrosinate side chain to coordinate the Fe centers. An important outcome is that the Sav host can regulate the Fe···Fe separation, which is known to be important for function in natural metalloproteins. Spectroscopic and structural studies from X-ray diffraction methods revealed uncommonly long Fe···Fe separations that change by less than 0.3 Å upon the binding of additional bridging ligands. The structural constraints imposed by the protein host on the di-Fe cores are unique and create examples of active sites having entatic states within engineered artificial metalloproteins.

Electronic State of the His/Tyr-Ligated Heme of BthA by Mössbauer and DFT Analysis.

The BthA protein from the microorganism Burkholderia thailandensis contains two hemes with axial His/OH2 and His/Tyr coordinations separated by the closest interheme distance of 14 Å. BthA has a similar structure and belongs to the same family of multiheme cytochrome c peroxidases as MauG, which performs long-range oxidation of the partner protein methylamine dehydrogenase. Magnetic Mössbauer spectroscopy of the diferric state of BthA corroborates previous structural work identifying a high-spin (His/OH2) peroxidatic heme and a low-spin (His/Tyr) electron transfer heme. Unlike MauG, addition of H2O2 fully converts the diferric form of BthA to a stable 2e- oxidized state, allowing a new assessment of this state. The peroxidatic heme is found to be oxidized to a canonical compound II, S = 1 oxoiron(IV) heme. In contrast, the electronic properties of the oxidized His/Tyr heme are puzzling. The isomer shift of the His/Tyr heme (0.17 mm/s) is close to that of the precursor S = 1/2 Fe3+ heme (0.21 mm/s) which suggests oxidation of the Tyr. However, the spin-dipolar hyperfine coupling constants are found here to be the same as those for the ferryl peroxidatic heme, indicating that the His/Tyr heme is also a compound II, S = 1 Fe4+ heme and ruling out oxidation of the Tyr. DFT calculations indicate that the unusually high isomer shift is not attributable to the rare axial His/Tyr heme coordination. The calculations are only compatible with spectroscopy for an unusually long Fe4+-OTyr distance, which is presumably under the influence of the protein environment of the His/Tyr heme moiety in the H2O2 oxidized state of the protein. The results offer new insights into how high valence intermediates can be tuned by the protein environment for performing long-range oxidation.

Kinetic and Spectroscopic Characterization of the Catalytic Ternary Complex of Tryptophan 2,3-Dioxygenase.

The first step of the kynurenine pathway for l-tryptophan (l-Trp) degradation is catalyzed by heme-dependent dioxygenases, tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase. In this work, we employed stopped-flow optical absorption spectroscopy to study the kinetic behavior of the Michaelis complex of Cupriavidus metallidurans TDO (cmTDO) to improve our understanding of oxygen activation and initial oxidation of l-Trp. On the basis of the stopped-flow results, rapid freeze-quench (RFQ) experiments were performed to capture and characterize this intermediate by Mössbauer spectroscopy. By incorporating the chlorite dismutase-chlorite system to produce high concentrations of solubilized O2, we were able to capture the Michaelis complex of cmTDO in a nearly quantitative yield. The RFQ-Mössbauer results confirmed the identity of the Michaelis complex as an O2-bound ferrous species. They revealed remarkable similarities between the electronic properties of the Michaelis complex and those of the O2 adduct of myoglobin. We also found that the decay of this reactive intermediate is the rate-limiting step of the catalytic reaction. An inverse α-secondary substrate kinetic isotope effect was observed with a kH/kD of 0.87 ± 0.03 when (indole-d5)-l-Trp was employed as the substrate. This work provides an important piece of spectroscopic evidence of the chemical identity of the Michaelis complex of bacterial TDO.

Effects of Noncovalent Interactions on High-Spin Fe(IV)-Oxido Complexes.

High-valent nonheme FeIV-oxido species are key intermediates in biological oxidation, and their properties are proposed to be influenced by the unique microenvironments present in protein active sites. Microenvironments are regulated by noncovalent interactions, such as hydrogen bonds (H-bonds) and electrostatic interactions; however, there is little quantitative information about how these interactions affect crucial properties of high valent metal-oxido complexes. To address this knowledge gap, we introduced a series of FeIV-oxido complexes that have the same S = 2 spin ground state as those found in nature and then systematically probed the effects of noncovalent interactions on their electronic, structural, and vibrational properties. The key design feature that provides access to these complexes is the new tripodal ligand [poat]3-, which contains phosphinic amido groups. An important structural aspect of [FeIVpoat(O)]- is the inclusion of an auxiliary site capable of binding a Lewis acid (LAII); we used this unique feature to further modulate the electrostatic environment around the Fe-oxido unit. Experimentally, studies confirmed that H-bonds and LAII s can interact directly with the oxido ligand in FeIV-oxido complexes, which weakens the Fe═O bond and has an impact on the electronic structure. We found that relatively large vibrational changes in the Fe-oxido unit correlate with small structural changes that could be difficult to measure, especially within a protein active site. Our work demonstrates the important role of noncovalent interactions on the properties of metal complexes, and that these interactions need to be considered when developing effective oxidants.

A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.

BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV)═O oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here, we show that installing a canonical Met ligand in lieu of the Tyr found at the heme of MauG associated with electron transfer, results in a construct that yields an unusually stable Fe(IV)═O porphyrin at the peroxidatic heme. This state is spontaneously formed at ambient conditions using either molecular O2 or H2O2. The resulting data illustrate how a ferryl iron, with unforeseen stability, may be achieved in biology.

Tuning the copper(II)/copper(I) redox potential for more robust copper-catalyzed C-N bond forming reactions.

Complexes of copper and 1,10-phenanthroline have been utilized for organic transformations over the last 50 years. In many cases these systems are impacted by reaction conditions and perform best under an inert atmosphere. Here we explore the role the 1,10-phenanthroline ligand plays on the electronic structure and redox properties of copper coordination complexes, and what benefit related ligands may provide to enhance copper-based coupling reactions. Copper(II) triflate complexes bearing 1,10-phenanthroline (phen), ([Cu(phen)2(OTf)]OTf, 1) and oxidized derivatives of phen including [Cu(edhp)2](OTf)2 (2), [Cu(pdo)2](OTf)2 (3), [Cu(dafo)2](OTf)2 (4) were prepared and characterized. X-ray crystallographic data show these related ligands subtly impacted the coordination geometry of the copper(II) ion. Complexes 1-3 had only incremental changes to the redox properties of the copper ions, complex 4 showed a drastically different redox potential affording a remarkably air stable copper(I) complex. These complexes 1-4 were then used to catalyze the C-N bond forming cross coupling between imidazole and various boronic acid substrates, where the increased stability of the copper(I) species in complex 4 appears to better support these CEL cross couplings.

Cytochrome c'ß-Met Is a Variant in the P460 Superfamily Lacking the Heme-Lysyl Cross-Link: A Peroxidase Mimic Generating a Ferryl Intermediate.

A defining characteristic of bacterial cytochromes (cyt's) in the P460 family is an unusual cross-link connecting the heme porphyrin to the side chain of a lysyl residue in the protein backbone. Here, via proteomics of the periplasmic fraction of the ammonia-oxidizing bacterium (AOB) Nitrosomonas europaea, we report the identification of a variant member of the P460 family that contains a methionyl residue in place of the cross-linking lysine. We formally designate this protein cytochrome "c'ß-Met" to distinguish it from other members bearing different residues at this position (e.g., cyt c'ß-Phe from the methane-oxidizing Methylococcus capsulatus Bath). As isolated, the monoheme cyt c'ß-Met is high-spin (S = 5/2). Optical spectroscopy suggests that a cross-link is absent. Hydroxylamine, the substrate for the cross-linked cyt P460 from N. europaea, did not appreciably alter the optical spectrum of cyt c'ß with up to 1000-fold excess at pH 7.5. Cyt c'ß-Met did however bind 1 equiv of H2O2, and with a slight excess, Mössbauer spectroscopy indicated the formation of a semistable ferryl (FeIV═O) Compound II-like species. The corresponding electron paramagnetic resonance showed a very low intensity signal indicative of a radical at g = 2.0. Furthermore, cyt c'ß-Met exhibited guaiacol-dependent peroxidase activity (kcat = 20.0 ± 1.2 s-1; KM = 2.6 ± 0.4 mM). Unlike cyt c'ß-Met, cyt P460 showed evidence of heme inactivation in the presence of 2 equiv of H2O2 with no appreciable guaiacol-dependent peroxidase activity. Mutagenesis of the cross-linking lysyl residue to an alanine in cyt P460, however, reversed this lack of activity.

Outer-Sphere Tyrosine 159 within the 3-Mercaptopropionic Acid Dioxygenase S-H-Y Motif Gates Substrate-Coordination Denticity at the Non-Heme Iron Active Site.

Thiol dioxygenases are non-heme mononuclear iron enzymes that catalyze the O2-dependent oxidation of free thiols (-SH) to produce the corresponding sulfinic acid (-SO2-). Regardless of the phylogenic domain, the active site for this enzyme class is typically comprised of two major features: (1) a mononuclear ferrous iron coordinated by three protein-derived histidines and (2) a conserved sequence of outer Fe-coordination-sphere amino acids (Ser-His-Tyr) spatially adjacent to the iron site (∼3 Å). Here, we utilize a promiscuous 3-mercaptopropionic acid dioxygenase cloned from Azotobacter vinelandii (Av MDO) to explore the function of the conserved S-H-Y motif. This enzyme exhibits activity with 3-mercaptopropionic acid (3mpa), l-cysteine (cys), as well as several other thiol-bearing substrates, thus making it an ideal system to study the influence of residues within the highly conserved S-H-Y motif (H157 and Y159) on substrate specificity and reactivity. The pKa values for these residues were determined by pH-dependent steady-state kinetics, and their assignments verified by comparison to H157N and Y159F variants. Complementary electron paramagnetic resonance and Mössbauer studies demonstrate a network of hydrogen bonds connecting H157-Y159 and Fe-bound ligands within the enzymatic Fe site. Crucially, these experiments suggest that the hydroxyl group of Y159 hydrogen bonds to Fe-bound NO and, by extension, Fe-bound oxygen during native catalysis. This interaction alters both the NO binding affinity and rhombicity of the 3mpa-bound iron-nitrosyl site. In addition, Fe coordination of cys is switched from thiolate only to bidentate (thiolate/amine) for the Y159F variant, indicating that perturbations within the S-H-Y proton relay network also influence cys Fe binding denticity.

Analysis of the Puzzling Exchange-Coupling Constants in a Series of Heterobimetallic Complexes.

The exchange-coupling constants (J) in a series of bimetallic complexes with an M2+(µ-OH)Fe3+ core (M = Mn, Fe, Ni, and Cu; series 1), which were reported in a recent study ( Sano et al. Inorg. Chem. 2017 , 56 , 14118 - 14128 ), have been analyzed with the help of density functional theory (DFT) calculations. The experimental J values of series 1 showed the remarkable property that they were virtually independent of metal M. This behavior contrasts with that observed for a related series of complexes with M2+Fe3+ cores reported by Chaudhuri and co-workers ( Biswas et al. Inorg. Chem. 2010 , 49 , 626 - 641 ) (series 2) in which J increases toward the upper end of the series. Broken symmetry DFT calculations for J, which yielded values in good agreement for the MnFe and NiFe complexes of series 1, gave for the CuFe complex a J value that was persistently much larger than that obtained from the experiment. Attempts to bridge the discrepancy by invoking various basis sets and corrections for hydrogen-bonding effects on J were not successful. The J values for series 1 were subsequently analyzed in the context of an exchange pathway model. From this analysis, it emerged that, in addition to the regular 2e-pathways, which contribute antiferromagnetic terms to J, there are also 3e-pathways that contribute ferromagnetic terms and have the propensity to keep J constant along series 1. It is shown that, while DFT evaluates the 2e-pathway terms reliably, this method seriously underestimates the 3e-pathway contributions, resulting in a too high J value for the CuFe complex of series 1. The pathway analysis of series 2 reveals that the 3e-pathway contributions to J are considerably smaller than those in series 1, resulting in J values that increase toward the upper end of the series, in accordance with the experiment.

A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.

Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H2O2) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we present the discovery of a unique diheme peroxidase BthA conserved in all Burkholderia. Using a combination of magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods, we report that BthA is capable of generating a bis-Fe(IV) species previously thought to be a unique feature of the diheme enzyme MauG. However, BthA is not MauG-like in that it catalytically converts H2O2 to water, and a 1.54-Å resolution crystal structure reveals striking differences between BthA and other superfamily members, including the essential residues for both bis-Fe(IV) formation and H2O2 turnover. Taken together, we find that BthA represents a previously undiscovered class of diheme enzymes, one that stabilizes a bis-Fe(IV) state and catalyzes H2O2 turnover in a mechanistically distinct manner.

A Synthetically Generated LFeIVOH n Complex.

High-valent Fe-OH species are important intermediates in hydroxylation chemistry. Such complexes have been implicated in mechanisms of oxygen-activating enzymes and have thus far been observed in Compound II of sulfur-ligated heme enzymes like cytochrome P450. Attempts to synthetically model such species have thus far seen relatively little success. Here, the first synthetic FeIVOH n complex has been generated and spectroscopically characterized as either [LFeIVOH]- or [LFeIVOH2]0, where H4L = Me4C2(NHCOCMe2NHCO)2CMe2 is a variant of a tetra-amido macrocyclic ligand (TAML). The steric bulk provided by the replacement of the aryl group with the -CMe2CMe2- unit in this TAML variant prevents dimerization in all oxidation states over a wide pH range, thus allowing the generation of FeIVOH n in near quantitative yield from oxidation of the [LFeIIIOH2]- precursor.

Controlling magnetism of Au133(TBBT)52 nanoclusters at single electron level and implication for nonmetal to metal transition.

The transition from the discrete, excitonic state to the continuous, metallic state in thiolate-protected gold nanoclusters is of fundamental interest and has attracted significant efforts in recent research. Compared with optical and electronic transition behavior, the transition in magnetism from the atomic gold paramagnetism (Au 6s1) to the band behavior is less studied. In this work, the magnetic properties of 1.7 nm [Au133(TBBT)52]0 nanoclusters (where TBBT = 4-tert-butylbenzenethiolate) with 81 nominal "valence electrons" are investigated by electron paramagnetic resonance (EPR) spectroscopy. Quantitative EPR analysis shows that each cluster possesses one unpaired electron (spin), indicating that the electrons fill into discrete orbitals instead of a continuous band, for that one electron in the band would give a much smaller magnetic moment. Therefore, [Au133(TBBT)52]0 possesses a nonmetallic electronic structure. Furthermore, we demonstrate that the unpaired spin can be removed by oxidizing [Au133(TBBT)52]0 to [Au133(TBBT)52]+ and the nanocluster transforms from paramagnetism to diamagnetism accordingly. The UV-vis absorption spectra remain the same in the process of single-electron loss or addition. Nuclear magnetic resonance (NMR) is applied to probe the charge and magnetic states of Au133(TBBT)52, and the chemical shifts of 52 surface TBBT ligands are found to be affected by the spin in the gold core. The NMR spectrum of Au133(TBBT)52 shows a 13-fold splitting with 4-fold degeneracy of 52 TBBT ligands, which are correlated to the quasi-D 2 symmetry of the ligand shell. Overall, this work provides important insights into the electronic structure of Au133(TBBT)52 by combining EPR, optical and NMR studies, which will pave the way for further understanding of the transition behavior in metal nanoclusters.