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PubMed1999

Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2[4Fe-4S] ferredoxin.

The ferredoxin from Chromatium vinosum (CvFd) exhibits sequence and structure peculiarities. Its two Fe4S4(SCys)4 clusters have unusually low potential transitions that have been unambiguously assigned here through NMR, EPR, and Mössbauer spectroscopy in combination with site-directed mutagenesis. The [4Fe-4S]2+/1+ cluster (cluster II) whose coordination sphere includes a two-turn loop between cysteines 40 and 49 was reduced by dithionite with an E degrees ' of -460 mV. Its S = 1/2 EPR signal was fast relaxing and severely broadened by g-strain, and its Mössbauer spectra were broad and unresolved. These spectroscopic features were sensitive to small perturbations of the coordination environment, and they were associated with the particular structural elements of CvFd, including the two-turn loop between two ligands and the C-terminal alpha-helix. Bulk reduction of cluster I (E degrees ' = -660 mV) was not possible for spectroscopic studies, but the full reduction of the protein was achieved by replacing valine 13 with glycine due to an approximately 60 mV positive shift of the potential. At low temperatures, the EPR spectrum of the fully reduced protein was typical of two interacting S = 1/2 [4Fe-4S]1+ centers, but because the electronic relaxation of cluster I is much slower than that of cluster II, the resolved signal of cluster I was observed at temperatures above 20 K. Contact-shifted NMR resonances of beta-CH2 protons were detected in all combinations of redox states. These results establish that electron transfer reactions involving CvFd are quantitatively different from similar reactions in isopotential 2[4Fe-4S] ferredoxins. However, the reduced clusters of CvFd have electronic distributions that are similar to those of clusters coordinated by the CysIxxCysIIxxCysIII.CysIVP sequence motif found in other ferredoxins with different biochemical properties. In all these cases, the electron added to the oxidized clusters is mainly accommodated in the pair of iron ions coordinated by CysII and CysIV.

Bacterial Proteins↗
PubMed1999

Purification and characterization of a tungsten-containing formate dehydrogenase from Desulfovibrio gigas.

An air-stable formate dehydrogenase (FDH), an enzyme that catalyzes the oxidation of formate to carbon dioxide, was purified from the sulfate reducing organism Desulfovibrio gigas (D. gigas) NCIB 9332. D. gigas FDH is a heterodimeric protein [alpha (92 kDa) and beta (29 kDa) subunits] and contains 7 +/- 1 Fe/protein and 0.9 +/- 0.1 W/protein. Selenium was not detected. The UV/visible absorption spectrum of D. gigas FDH is typical of an iron-sulfur protein. Analysis of pterin nucleotides yielded a content of 1.3 +/- 0.1 guanine monophosphate/mol of enzyme, which suggests a tungsten coordination with two molybdopterin guanine dinucleotide cofactors. Both Mössbauer spectroscopy performed on D. gigas FDH grown in a medium enriched with (57)Fe and EPR studies performed in the native and fully reduced state of the protein confirmed the presence of two [4Fe-4S] clusters. Variable-temperature EPR studies showed the presence of two signals compatible with an atom in a d(1) configuration albeit with an unusual relaxation behavior as compared to the one generally observed for W(V) ions.

Aerobiosis↗
PubMed1999

Mössbauer and electron paramagnetic resonance studies of the cytochrome bf complex.

The (57)Fe-enriched cytochrome bf complex has been isolated from hydrocultures of spinach. It has been studied at different redox states by optical, EPR, and Mössbauer spectroscopy. The Mössbauer spectrum of the native complex at 190 K with all iron centers in the oxidized state reveals the presence of four different iron sites: low-spin ferric iron in cytochrome b [with an isomer shift (delta) of 0.20 mm/s, a quadrupole splitting (DeltaE(Q)) of 1.77 mm/s, and a relative area of 40%], low-spin ferric iron of cytochrome f (delta = 0.26 mm/s, DeltaE(Q) = 1.90 mm/s, and a relative area of 20%), and two high-spin ferric iron sites of the Rieske iron-sulfur protein (ISP) with a bis-cysteine and a bis-histidine ligated iron (delta(1) = 0.15 mm/s, DeltaE(Q1) = 0.70 mm/s, and a relative area of 20%, and delta(2) = 0.25 mm/s, DeltaE(Q2) = 0.90 mm/s, and a relative area of 20%, respectively). EPR and magnetic Mössbauer measurements at low temperatures corroborate these results. A crystal-field analysis of the EPR data and of the magnetic Mössbauer data yields estimates for the g-tensors (g(z)(), g(y)(), and g(x)()) of cytochrome b (3.60, 1.35, and 1.1) and of cytochrome f (3.51, 1.69, and 0.9). Addition of ascorbate reduces not only the iron of cytochrome f to the ferrous low-spin state (delta = 0.43 mm/s, DeltaE(Q) = 1.12 mm/s at 4.2 K) but also the bis-histidine coordinated iron of the Rieske 2Fe-2S center to the ferrous high-spin state (delta(2) = 0.73 mm/s, DeltaE(Q2) = -2.95 mm/s at 4.2 K). At this redox step, the Mössbauer parameters of cytochrome b have not changed, indicating that the redox changes of cytochrome f and the Rieske protein did not change the first ligand sphere of the low-spin ferric iron in cytochrome b. Reduction with dithionite further reduces the two hemes of cytochrome b to the ferrous low-spin state (delta = 0.49 mm/s, DeltaE(Q) = 1.08 mm/s at 4.2 K). The spin Hamiltonian analysis of the magnetic Mössbauer spectra at 4.2 K yields hyperfine parameters of the reduced Rieske 2Fe-2S center in the cytochrome bf complex which are very similar to those reported for the Rieske center from Thermus thermophilus [Fee, J. A., Findling, K. L., Yoshida, T., et al. (1984) J. Biol. Chem. 259, 124-133].

Ascorbic Acid↗
PubMed1999

Stages in iron storage in the ferritin of Escherichia coli (EcFtnA): analysis of Mössbauer spectra reveals a new intermediate.

Iron uptake into the nonheme ferritin of Escherichia coli (EcFtnA) and its site-directed variants have been investigated by Mössbauer spectroscopy. EcFtnA, like recombinant human H chain ferritin (HuHF), oxidized Fe(II) at a dinuclear ferroxidase center situated at a central position within each subunit. As with HuHF, Mössbauer subspectra observed between 1 min and 24 h after Fe(II) addition were assigned to Fe(III) monomers, "c", mu-oxo-bridged dimers, "b", and clusters, "a", the latter showing magnetically split spectra, "d", at 4.1 K. Like those of HuHF, the mu-oxo-bridged dimers were formed at the ferroxidase centers. However, the analysis also revealed the presence of a new type of dimer, "e" (QS1 = 0.38 mm/s, IS1 = 0.51 mm/s and QS2 = 0.72 mm/s, IS2 = 0.50 mm/s), and this was also assigned to the ferroxidase center. Dimers "b" appeared to be converted to dimers "e" over time. Subspectra "e" became markedly asymmetric at temperatures above 90 K, suggesting that the two Fe(III) atoms of dimers "e" were more weakly coupled than in the mu-oxo-bridged dimers "b", possibly due to OH- bridging. Monomeric Fe(III), giving relaxation spectra "c", was assigned to a unique site C that is near the dinuclear center. In EcFtnA all three iron atoms seemed to be oxidized together. In contrast to HuHF, no Fe(III) clusters were observed 24 h after the aerobic addition of 48 Fe(II) atoms/molecule in wild-type EcFtnA. This implies that iron is more evenly distributed between molecules in the bacterial ferritins, which may account for its greater accessibility.

Alanine↗
PubMed1999

Mössbauer studies of the formation and reactivity of a quasi-stable peroxo intermediate of stearoyl-acyl carrier protein Delta 9-desaturase.

Stearoyl-ACP Delta(9)-desaturase (Delta 9D) is a diiron enzyme that catalyzes 18:0-ACP desaturation. Each subunit of homodimeric resting Delta 9D contains a diferric cluster, while chemical reduction by 4e(-) produces a diferrous cluster in each subunit. Reaction of 4e(-)-reduced Delta 9D with 18:0-ACP and O(2) yields a blue chromophore (lambda(max) approximately 700 nm) that exhibits a vibrational spectrum indicative of a micro-1,2-peroxo complex; this species has been designated peroxo Delta9D. In contrast to other enzymic peroxodiiron intermediates, peroxo Delta 9D is long-lived (t(1/2) approximately 30 min at 25 degrees C) and decays via an oxidase reaction without formation of either H(2)O(2) or product (18:1-ACP). In this work, optical, transient kinetic, and Mössbauer techniques have been used to further investigate the origin and nature of this unusual peroxodiiron complex. Rapid mixing of 4e(-) Delta 9D with O(2)-equilibrated 18:0-ACP produced peroxo Delta 9D as revealed by a temperature-dependent, pseudo-first-order absorption increase at 700 nm (k = 46 s(-)(1) at 6 degrees C). The Mössbauer spectrum of peroxo Delta 9D, accounting for 96% of the total iron, consists of two quadrupole doublets present in equal proportions: delta(1) = 0.68(1) mm/s, and Delta E(Q)(1) = 1.90(2) mm/s; delta(2) = 0.64(1) mm/s, and Delta E(Q)(2) = 1.06(2) mm/s. Decay of the 700 nm optical band (k = 0.004 min(-)(1) at 6 degrees C) correlates with the complete conversion of peroxo Delta 9D into a complex called peroxo-cycled Delta 9D, which exhibits two new doublets present in equal proportions: delta(1) = 0.57(2) mm/s, and Delta E(Q)(1) = 1. 91(3) mm/s; delta(2) = 0.52(2) mm/s, and Delta E(Q)(2) = 1.41(3) mm/s. Thus, peroxo Delta 9D contains two asymmetric diferric clusters and reacts to yield peroxo-cycled Delta 9D, also containing two asymmetric diferric clusters that most probably represent a substrate complex state. The clusters of both peroxo Delta 9D and peroxo-cycled Delta 9D have a diamagnetic ground state. Because peroxo Delta 9D and peroxo-cycled Delta 9D are observed only in the presence of 18:0-ACP, substrate binding appears to have introduced asymmetry into the Delta 9D diiron clusters. In situ photolysis of peroxo Delta 9D at 4.2 K in the Mössbauer cryostat caused the release of O(2) and the reappearance of a diferrous Delta 9D.18:0-ACP complex with slightly changed parameters, suggesting a constrained cluster configuration was produced by the photolysis event. Annealing the photolyzed sample for 30 min at 77 K quantitatively restored the Mössbauer spectrum of peroxo Delta 9D, showing that the released O(2) was effectively sequestered within the active site.

Fatty Acid Desaturases↗
PubMedDate not supplied

A Mössbauer study of the interaction of chitosan and D-glucosamine with iron and its relevance to other metalloenzymes.

The interaction of iron with water-soluble polymer chitosan and monomer d-glucosamine is investigated by Mössbauer spectroscopy. The 4.2 K Mössbauer spectrum of Fe-water-soluble chitosan complex indicates the presence of a magnetic pattern and a quadrupole doublet, and analysis of the spectral data leads to the conclusion that an Fe(II) state is partially stabilized in this system. Fe-glucosamine (monomer of chitosan) complex, on the other hand, clearly stabilizes the Fe(II) state in the acidic pH range as evidenced from the isomer shift extracted from the Mössbauer spectra. The oxidation state of the metal ion in the complex is found to be pH dependent. Indirect evidence supporting the involvement of amino group in the bonding with the metal ion is discussed. From the analysis of the experimental data under varying experimental conditions, it is concluded that the metal ion in the complex is at least tetracoordinated and at most hexacoordinated with O/N ligands of the polymer or monomer and thus corroborates the bonding scheme proposed earlier.

Chitin↗
PubMed2005

Influence of sediment bioreduction and reoxidation on uranium sorption.

The influence of sediment bioreduction and reoxidation on U(VI) sorption was studied using Fe(II) oxide-containing saprolite from the U.S. Department of Energy (DOE) Oak Ridge site. Bioreduced sediments were generated by anoxic incubation with a metal-reducing bacterium, Shewanella putrefaciens strain CN32, supplied with lactate as an electron donor. The reduced sediments were subsequently reoxidized by air contact. U(VI) sorption was studied in NaNO3-HCO3 electrolytes that were both closed and open to atmosphere and where pH, U(VI), and carbonate concentration were varied. Mössbauer spectroscopy and chemical analyses showed that 50% of the Fe(III)-oxides were reduced to Fe(II) that was sorbed to the sediment during incubation with CN32. However, this reduction and subsequent reoxidation of the sorbed Fe(II) had negligible influence on the rate and extent of U sorption or the extractability of sorbed U by 0.2 mol/L NaHCO3. Various results indicated that U(VI) surface complexation was the primary process responsible for uranyl sorption by the bioreduced and reoxidized sediments. A two-site, nonelectrostatic surface complexation model best described U(VI) adsorption under variable pH, carbonate, and U(VI) conditions. A ferrihydrite-based diffuse double layer model provided a better estimation of U(VI) adsorption without parameter adjustment than did a goethite-based model, even though a majority of the Fe(III)-oxides in the sediments were goethite. Our results highlight the complexity of the coupled U-Fe redox system and show that sorbed Fe(II) is not a universal reductant for U(VI) as commonly assumed.

Adsorption↗
PubMed2004

Spectroscopic evidence for Fe(II)-Fe(III) electron transfer at the iron oxide-water interface.

Using the isotope specificity of 57Fe Mössbauer spectroscopy, we report spectroscopic observations of Fe(II) reacted with oxide surfaces under conditions typical of natural environments (i.e., wet, anoxic, circumneutral pH, and about 1% Fe(II)). Mössbauer spectra of Fe(II) adsorbed to rutile (TiO2) and aluminum oxide (Al2O3) show only Fe(II) species, whereas spectra of Fe(II) reacted with goethite (alpha-FeOOH), hematite (alpha-Fe2O3), and ferrihydrite (Fe5HO8) demonstrate electron transfer between the adsorbed Fe(II) and the underlying iron(III) oxide. Electron-transfer induces growth of an Fe(III) layer on the oxide surface that is similar to the bulk oxide. The resulting oxide is capable of reducing nitrobenzene (as expected based on previous studies), but interestingly, the oxide is only reactive when aqueous Fe(II) is present. This finding suggests a novel pathway for the biogeochemical cycling of Fe and also raises important questions regarding the mechanism of contaminant reduction by Fe(II) in the presence of oxide surfaces.

Adsorption↗
PubMed2006

Mineralogy and characterization of arsenic, iron, and lead in a mine waste-derived fertilizer.

The solid-state speciation of arsenic (As), iron (Fe), and lead (Pb) was studied in the mine waste-derived fertilizer Ironite using X-ray absorption spectroscopy, Mössbauer spectroscopy, and aging studies. Arsenic was primarily associated with ferrihydrite (60-70%), with the remainder found in arsenopyrite (30-40%). Lead was observed almost exclusively as anglesite (PbSO4), with <1% observed as galena (PbS). The identification of As in oxidized Fe oxides and Pb as PbSO4 is in disagreement with the dominant reduced phases previously reported and suggests As and Pb contained within the mine waste-derived product are more bioavailable than previously considered. Aging studies in solution result in Ironite granules separating into two distinct fractions, an orange oxide precipitate and a crystalline fraction with a metallic luster. The orange oxide fraction contained As adsorbed/precipitated with ferrihydrite that is released into solution when allowed to equilibrate with water. The fraction with a metallic luster contained pyrite and arsenopyrite. A complete breakdown of arsenopyrite was observed in Ironite aged for 1 month in buffered deionized water. The observations from this study indicate As and Pb exist as oxidized phases that likely develop from the beneficiation and processing of mine tailings for commercial sale. The potential release of As and Pb has important implications for water quality standards and human health. Of particular concern is the quantity of As released from mine waste-derived products due to the new As regulation applied in 2006, limiting As levels to 10 microg L(-1) in drinking water.

Adsorption↗
PubMed2001

Spectroscopic studies on iron complexes of different anthracyclines in aprotic solvent systems.

Iron complexes of daunorubicin, idarubicin, pirarubicin, and doxorubicin in anhydrous DMF were studied by UV/vis, CD, fluorescence, Mössbauer, and EPR spectroscopy. Titration studies of the metal-free anthracyclines showed one (UV-detectable) deprotonation step requiring 2 equiv of base, compared to 1 equiv for quinizarine. Metal complexation was studied at three different metal/ligand ratios, and with increasing amounts of base. The results obtained from optical spectroscopy show the existence of two different complex species and give clear indications for the requirements of metal complexation. Complex species I, formed at a low iron-to-ligand ratio, is less dependent on base addition than complex species II formed with equimolar ferric ion. EPR and Mössbauer experiments provide further insight into the structures of both complex species. Lack of spin density of the Mössbauer samples in EPR indicates spin coupling between the metal centers. Mössbauer spectra consist of single quadrupole doublets with values typical for high-spin ferric ion in an octahedral arrangement. The Mössbauer spectroscopic features at 7 T exclude the presence of S = 0 dimers. Complex I represents a monomeric ferric iron complex whereas complex II is consistent with a more or less aggregrated oligomeric Fe-anthracycline system.

Antibiotics, Antineoplastic↗
PubMed2001

Molybdenum-iron-sulfur clusters of nuclearities eight and sixteen, including a topological analogue of the P-cluster of nitrogenase.

Transformations of the edge-bridged double cubane cluster [(Cl4cat)2(Et3P)2Mo2Fe6S8(PEt3)4] (1) under reducing conditions have been investigated as synthetic approaches to the clusters of nitrogenase. Cluster 1 is a versatile precursor to different Mo-Fe-S cluster types. The reaction system 1/K(C14H10) in THF yields the reduced cluster [(Cl4cat)2(Et3P)2Mo2Fe6S8(PEt3)4]1- (2), which as its crystalline Et4N+ salt retains the edge-bridged structure of 1. X-ray structural and Mössbauer spectroscopic results indicate an unsymmetrical electron distribution with localized [MoFe3S4]2+,1+ cubane-type units. The system 1/2K(C14H10)/2HS- in THF/acetonitrile affords [(Cl4cat)4(Et3P)4Mo4Fe12S20K3(DMF)]5- (3), whose structure was determined as the Ph3PMe+ salt. The cluster consists of two isostructural Mo2Fe6S9 fragments connected by two mu 2-S bridges. Three potassium ions are bound between the two fragments. In each fragment, the iron atoms are present in tetrahedral FeS4 and the molybdenum atoms in octahedral MoO2PS3 coordination units, and two MoFe3(mu 3-S)3 cuboidal units are bridged by a common mu 6-S atom. The fragments have idealized mirror symmetry and are isostructural with two of the fragments present in the previously reported high-nuclearity cluster [(Cl4cat)6(Et3P)6Mo6Fe20S30]8- (4) (Osterloh, F.; Sanakis, Y.; Staples, R. J.; Münck, E.; Holm, R. H. Angew. Chem., Int. Ed. Engl. 1999, 38, 2066). On the basis of overall shape, atom connectivities, and metric features, the Mo2Fe6S9 fragment is a topological analogue of the P-cluster of nitrogenase in the PN (reduced) state. A third cluster type, formed as a minor byproduct in the reaction system leading to 2, was crystallographically identified as [(Cl4cat)2(Et3P)2Mo2Fe6S8(PEt3)4]4-, whose core is made up of two MoFe3(mu 3-S)3 cuboidal units bridged by two mu 2-S atoms and connected by a direct Fe-Fe bond. Full structural details and the redox properties of 2 and 3 are reported.

Crystallography, X-Ray↗
PubMed2000

Structural and electronic characterization of nitrosyl(octaethylporphinato)iron(III) perchlorate derivatives.

The synthesis and crystallographic characterization of the five-coordinate iron(III) porphyrinate complex [Fe(OEP)(NO)]ClO4 are reported. This [FeNO]6 complex has a nearly linear Fe-N-O group (angle = 173.19(13) degrees) with a small off-axis tilt of the Fe-N(NO) vector from the heme normal (angle = 4.6 degrees); the Fe-N(NO) distance is 1.6528(13) A and the iron is displaced 0.32 A out-of-plane. The complex forms a tight cofacial pi-pi dimer in the solid state. Mössbauer spectra for this derivative as well as for a related crystalline form are measured both in zero applied magnetic field and in a 7 T applied field. Fits to the measurements made in applied magnetic field demonstrate that both crystalline forms of [Fe(OEP)(NO)]ClO4 have a diamagnetic ground state at 4.2 K. The observed isomer shifts (delta = 0.22-0.24 mm/s) are smaller than those typically observed for low-spin iron(III) porphyrinates. Analogous Mössbauer measurements are also obtained for a six-coordinate derivative, [Fe(OEP)(Iz)(NO)]ClO4 (Iz = indazole). The observed isomer shift for this species is smaller still (delta = 0.02 mm/s). All derivatives show a strong temperature dependence of the isomer shift. The data emphasize the strongly covalent nature of the FeNO group. The Mössbauer isomer shifts suggest formal oxidation states greater than +3 for iron, but the NO stretching frequencies are not consistent with such a large charge transfer to NO. Differences in the observed nitrosyl stretching frequencies of the two crystalline forms of [Fe(OEP)(NO)]ClO4 are discussed.

Crystallography, X-Ray↗
PubMed2001

Synthesis and electrochemical studies of diiron complexes of 1,8-naphthyridine-based dinucleating ligands to model features of the active sites of non-heme diiron enzymes.

A bis(mu-carboxylato)(mu-1,8-naphthyridine)diiron(II) complex, [Fe2(BPMAN)(mu-O2CPhCy)2](OTf)2 (1), was prepared by using the 1,8-naphthyridine-based dinucleating ligand BPMAN, where BPMAN = 2,7-bis[bis(2-pyridylmethyl)aminomethyl]-1,8-naphthyridine. The cyclic voltammogram (CV) of this complex in CH2Cl2 exhibited two reversible one-electron redox waves at +296 mV (DeltaE(p) = 80 mV) and +781 mV (DeltaE(p) = 74 mV) vs Cp2Fe+/Cp2Fe, corresponding to the FeIIIFeII/FeIIFeII and FeIIIFeIII/FeIIIFeII couples, respectively. This result is unprecedented for diiron complexes having no single atom bridge. Dinuclear complexes [Fe2(BPMAN)(mu-OH)(mu-O2CPhCy)](OTf)2 (2) and [Mn2(BPMAN)(mu-O2CPhCy)2](OTf)2 (3) were also synthesized and structurally characterized. The cyclic voltammogram of 2 in CH2Cl2 exhibited one reversible redox wave at -22 mV only when the potential was kept below +400 mV. The CV of 3 showed irreversible oxidation at potentials above +900 mV. Diiron(II) complexes [Fe2(BEAN)(mu-O2CPhCy)3](OTf) (4) and [Fe2(BBBAN)(mu-OAc)2(OTf)](OTf) (6) were also prepared and characterized, where BEAN = 2,7-bis(N,N-diethylaminomethyl)-1,8-naphthyridine and BBBAN = 2,7-bis[2-[2-(1-methyl)benzimidazolylethyl]-N-benzylaminomethyl]-1,8-naphthyridine. The cyclic voltammograms of these complexes were recorded. The Mössbauer properties of the diiron compounds were studied.

Binding Sites↗
PubMed2001

Synthesis and spectroscopic studies of non-heme diiron(III) species with a terminal hydroperoxide ligand: models for hemerythrin.

Two compounds, [Fe2(mu-OH)(mu-Ph4DBA)(TMEDA)2(OTf)] (4) and [Fe2(mu-OH)(mu-Ph4DBA)(DPE)2(OTf)] (7), where Ph4DBA(2-) is the dinucleating bis(carboxylate) ligand dibenzofuran-4,6-bis(diphenylacetate), have been prepared as synthetic models for the dioxygen-binding non-heme diiron protein hemerythrin (Hr). X-ray crystallography reveals that, in the solid state, these compounds contain the asymmetric coordination environment found at the diiron center in the reduced form of the protein, deoxyHr. Mössbauer spectra of the models (4, delta = 1.21(2), DeltaE(Q) = 2.87(2) mm s(-1); 7, delta(av) = 1.23(1), DeltaE(Qav) = 2.79(1) mm s(-1)) and deoxyHr (delta = 1.19, DeltaE(Q) = 2.81 mm s(-1)) are also in good agreement. Oxygenation of the diiron(II) complexes dissolved in CH2Cl2 containing 3 equiv of N-MeIm (4) or neat EtCN (7) at -78 degrees C affords a red-orange solution with optical bands at 336 nm (7300 M(-1) cm(-1)) and 470 nm (2600 M(-1) cm(-1)) for 4 and at 334 nm (6400 M(-1) cm(-1)) and 484 nm (2350 M(-1) cm(-1)) for 7. These spectra are remarkably similar to that of oxyHr, 330 nm (6800 M(-1) cm(-1)) and 500 nm (2200 M(-1) cm(-1)). The electron paramagnetic resonance (EPR) spectrum of the cryoreduced, mixed-valence dioxygen adduct of 7 displays properties consistent with a (mu-oxo)diiron(II,III) core. An investigation of 7 and its dioxygen-bound adduct by extended X-ray absorption fine structure (EXAFS) spectroscopy indicates that the oxidized species contains a (mu-oxo)diiron(III) core with iron-ligand distances in agreement with those expected for oxide, carboxylate, and amine/hydroperoxide donor atoms. The analogous cobalt complex [Co2(mu-OH)(mu-Ph4DBA)(TMEDA)2(OTf)] (6) was synthesized and structurally characterized, but it was unreactive toward dioxygen.

Crystallography, X-Ray↗
PubMed2001

Influence of extrinsic factors on electron transfer in a mixed-valence Fe(2+)/Fe(3+) complex: experimental results and theoretical considerations.

The crystal structure of the mixed-valence complex (NEt(4))[Fe(2)(salmp)(2)].xMeCN(crystal) (x = 2,3) [1].xMeCN(crystal) was determined at temperatures between 153 and 293 K. The complex shows distinct Fe(2+) and Fe(3+) sites over this temperature interval. Variable temperature Mössbauer spectra confirm the valence-localized character of the complex. In contrast, spectroscopic investigation of powder samples generated from [1].xMeCN(crystal) indicate the presence of a valence-averaged component at temperatures above 150 K. To elucidate this apparent contradiction we have conducted a variable-temperature Mössbauer investigation of different forms of 1, including [1].xMeCN(crystal), [1].2DMF(crystal), [1].yMeCN(powder), and solution samples of 1 in acetonitrile. The low-temperature Mössbauer spectra of all forms are virtually identical and confirm the valence-localized nature of the S = (9)/(2) ground state. The high-temperature spectra reveal a subtle control of electron hopping by the environment of the complexes. Thus, [1].xMeCN(crystal) has valence-localized spectra at all explored temperatures, [1].2DMF(crystal) exhibits a complete collapse into a valence-averaged spectrum over a narrow temperature range, the powder exhibits partial valence averaging over a broad temperature interval, and the solution sample shows at 210 K the presence of a valence-averaged component in a minor proportion. The spectral transformations are characterized by a coexistence of valence-localized and valence-averaged spectral components. This phenomenon cannot be explained by intramolecular electron hopping between the valence-localized states Fe(A)(2+)Fe(B)(3+) and Fe(A)(3+)Fe(B)(2+) in a homogeneous ensemble of complexes, but requires relaxation processes involving at least three distinguishable states of the molecular anion. Hopping rates for [1].2DMF(crystal) and [1].yMeCN(powder) have been determined from spectral simulations, based on stochastic line shape theory. Analysis of the temperature dependences of the transfer rates reveals the existence of thermally activated processes between (quasi) degenerate excited states in both forms. The preexponential factors in the rate law for the hopping processes in the [1].yMeCN(powder) and [1].2DMF(crystal) differ dramatically and suggest an important influence of the asymmetry of the complex environment (crystal) on intramolecular electron hopping. The differences between the spectra for the crystalline sample [1].xMeCN and those for powders generated under vacuum from these crystals indicate that solvate depletion has a profound effect on the dynamic behavior. Finally, two interpretations for the three states involved in the relaxation processes in 1 are given and critically discussed (salmp = bis(salicyledeneamino)-2-methylphenolate(3-)).

Crystallography, X-Ray↗
PubMed2002

Single- and double-cubane clusters in the multiple oxidation states [VFe(3)S(4)](3+,2+,1+).

A new series of cubane-type [VFe(3)S(4)](z)() clusters (z = 1+, 2+, 3+) has been prepared as possible precursor species for clusters related to those present in vanadium-containing nitrogenase. Treatment of [(HBpz(3))VFe(3)S(4)Cl(3)](2)(-) (2, z = 2+), protected from further reaction at the vanadium site by the tris(pyrazolyl)hydroborate ligand, with ferrocenium ion affords the oxidized cluster [(HBpz(3))VFe(3)S(4)Cl(3)](1)(-) (3, z = 3+). Reaction of 2 with Et(3)P results in chloride substitution to give [(HBpz(3))VFe(3)S(4)(PEt(3))(3)](1+) (4, z = 2+). Reaction of 4 with cobaltocene reduced the cluster with formation of the edge-bridged double-cubane [(HBpz(3))(2)V(2)Fe(6)S(8)(PEt(3))(4)] (5, z = 1+, 1+), which with excess chloride underwent ligand substitution to afford [(HBpz(3))(2)V(2)Fe(6)S(8)Cl(4)](4)(-) (6, z = 1+, 1+). X-ray structures of (Me(4)N)[3], [4](PF(6)), 5, and (Et(4)N)(4)[6] x 2MeCN are described. Cluster 5 is isostructural with previously reported [(Cl(4)cat)(2)(Et(3)P)(2)Mo(2)Fe(6)S(8)(PEt(3))(4)] and contains two VFe(3)S(4) cubanes connected across edges by a Fe(2)S(2) rhomb in which the bridging Fe-S distances are shorter than intracubane Fe-S distances. Mössbauer (2-5), magnetic (2-5), and EPR (2, 4) data are reported and demonstrate an S = 3/2 ground state for 2 and 4 and a diamagnetic ground state for 3. Analysis of (57)Fe isomer shifts based on an empirical correlation between shift and oxidation state and appropriate reference shifts results in two conclusions. (i) The oxidation 2 --> 3 + e(-) results in a change in electron density localized largely or completely on the Fe(3) subcluster and associated sulfur atoms. (ii) The most appropriate charge distributions are [V(3+)Fe(3+)Fe(2+)(2)S(4)](2+) (Fe(2.33+)) for 1, 2, and 4 and [V(3+)Fe(3+)(2)Fe(2+)S(4)](3+) (Fe(2.67+)) for 3 and [V(2)Fe(6)S(8)(SEt)(9)](3+). Conclusion i applies to every MFe(3)S(4) cubane-type cluster thus far examined in different redox states at parity of cluster ligation. The formalistic charge distributions are regarded as the best current approximations to electron distributions in these delocalized species. The isomer shifts require that iron atoms are mixed-valence in each cluster.

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