Abstract Metglas 2605S3, having a nominal composition of Fe79B16Si5, has been studied by 57Fe Mossbauer spectroscopy over a temperature range of 77–900 K. The analysis of the distribution of hyperfine fields indicates two peaks. The Curie... more
Abstract Metglas 2605S3, having a nominal composition of Fe79B16Si5, has been studied by 57Fe Mossbauer spectroscopy over a temperature range of 77–900 K. The analysis of the distribution of hyperfine fields indicates two peaks. The Curie and the crystallization temperatures are found to be 730 and 829 K, respectively, by zero velocity counting method. The reduced hyperfine field vs reduced temperature data deviate from the theoretical Brillouin curve and the deviation is explained by the modified Handrich's expression. The existence of spin waves of longer wavelength have been confirmed.
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Desulfoferrodoxin, a non-heme iron protein, was purified previously from extracts of Desulfovibrio desulfuricans (ATCC 27774) (Moura, I., Tavares, P., Moura, J. J. G., Ravi, N., Huynh, B. H., Liu, M.-Y., and LeGall, J. (1990) J. Biol.... more
Desulfoferrodoxin, a non-heme iron protein, was purified previously from extracts of Desulfovibrio desulfuricans (ATCC 27774) (Moura, I., Tavares, P., Moura, J. J. G., Ravi, N., Huynh, B. H., Liu, M.-Y., and LeGall, J. (1990) J. Biol. Chem. 265, 21596-21602). The as-isolated protein displays a pink color (pink form) and contains two mononuclear iron sites in different oxidation states: a ferric site (center I) with a distorted tetrahedral sulfur coordination similar to that found in desulforedoxin from Desulfovibrio gigas and a ferrous site (center II) octahedrally coordinated with predominantly nitrogen/oxygen-containing ligands. A new form of desulfoferrodoxin which displays a gray color (gray form) has now been purified. Optical, electron paramagnetic resonance (EPR), and Mössbauer data of the gray desulfoferrodoxin indicate that both iron centers are in the high-spin ferric states. In addition to the EPR signals originating from center I at g = 7.7, 5.7, 4.1, and 1.8, the gray form of desulfoferrodoxin exhibits a signal at g = 4.3 and a shoulder at g = 9.6, indicating a high-spin ferric state with E/D approximately 1/3 for the oxidized center II. Redox titrations of the gray form of the protein monitored by optical spectroscopy indicate midpoint potentials of +4 +/- 10 and +240 +/- 10 mV for centers I and II, respectively. Mössbauer spectra of the gray form of the protein are consistent with the EPR finding that both centers are high-spin ferric and can be analyzed in terms of the EPR-determined spin Hamiltonian parameters. The Mössbauer parameters for both the ferric and ferrous forms of center II are indicative of a mononuclear high spin iron site with octahedral coordination and predominantly nitrogen/oxygen-containing ligands. Resonance Raman studies confirm the structural similarity of center I and the distorted tetrahedral FeS4 center in desulforedoxin and provide evidence for one or two cysteinyl-S ligands for center II. On the basis of the resonance Raman results, the 635 nm absorption band that is responsible for the gray color of the oxidized protein is assigned to a cysteinyl-S-->Fe(III) charge transfer transition localized on center II. The novel properties and possible function of center II are discussed in relation to those of mononuclear iron centers in other enzymes.
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Research Interests: Chemistry, Biological Chemistry, Medicine, Biological Sciences, Biological, and 15 moreIron, CHEMICAL SCIENCES, Amino Acids, Spectrum analysis, Repetitive Strain Injury, Rubredoxin, Molecular weight, Amino Acid Sequence, Ferrous, Oxidation-Reduction, Desulfovibrio, Biochemistry and cell biology, Molecular Sequence Data, Medical and Health Sciences, and Medical biochemistry and metabolomics
Page 1. J. Am. Chem. SOC. 1994,116, 8015-8023 8015 Mechanism of Assembly of the Tyrosyl Radical-Diiron( 111) Cofactor of E. coli Ribonucleotide Reductase. 2. Kinetics of The Excess Fe2+ Reaction by Optical, EPR, and Mossbauer... more
Page 1. J. Am. Chem. SOC. 1994,116, 8015-8023 8015 Mechanism of Assembly of the Tyrosyl Radical-Diiron( 111) Cofactor of E. coli Ribonucleotide Reductase. 2. Kinetics of The Excess Fe2+ Reaction by Optical, EPR, and Mossbauer Spectroscopies ...
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From low-temperature Mössbauer measurement on FeC2O4·2D2O the reported difference in quadrupole splitting from the simple dihydrate is inferred to be due to lattice effects. The Zeeman split spectrum has been analyzed taking into account... more
From low-temperature Mössbauer measurement on FeC2O4·2D2O the reported difference in quadrupole splitting from the simple dihydrate is inferred to be due to lattice effects. The Zeeman split spectrum has been analyzed taking into account the ‘ambiguity problem’ and the hyperfine parameters were determined to be I.S.=1.22 mm/sec; Q.S.=1.93 mm/sec; ?=0.65 to 0.72; ?=90 to 83.1o and ?=0 to 11.8o. The principal electric field gradient axis lies along the crystal a-axis with VYY and $$\mathop H\limits^ \to$$ lying along the crystal b-axis. The crystal field parameters 10Dq, Ds and Dt have been determined to be ~ 10500, ~ 185 and ~ 211 cm-1, respectively.
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Page 1. J. Am. Chem. SOC. 1994,116, 8015-8023 8015 Mechanism of Assembly of the Tyrosyl Radical-Diiron( 111) Cofactor of E. coli Ribonucleotide Reductase. 2. Kinetics of The Excess Fe2+ Reaction by Optical, EPR, and Mossbauer... more
Page 1. J. Am. Chem. SOC. 1994,116, 8015-8023 8015 Mechanism of Assembly of the Tyrosyl Radical-Diiron( 111) Cofactor of E. coli Ribonucleotide Reductase. 2. Kinetics of The Excess Fe2+ Reaction by Optical, EPR, and Mossbauer Spectroscopies ...
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Page 1. J. Am. Chem. SOC. 1994,116, 8015-8023 8015 Mechanism of Assembly of the Tyrosyl Radical-Diiron( 111) Cofactor of E. coli Ribonucleotide Reductase. 2. Kinetics of The Excess Fe2+ Reaction by Optical, EPR, and Mossbauer... more
Page 1. J. Am. Chem. SOC. 1994,116, 8015-8023 8015 Mechanism of Assembly of the Tyrosyl Radical-Diiron( 111) Cofactor of E. coli Ribonucleotide Reductase. 2. Kinetics of The Excess Fe2+ Reaction by Optical, EPR, and Mossbauer Spectroscopies ...
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The synthesis of appropriate transition-metal complexes to model the structural, spectroscopic, and magnetic properties of a metalloprotein active-site provides an opportunity to consider the function and associated mechanism of that... more
The synthesis of appropriate transition-metal complexes to model the structural, spectroscopic, and magnetic properties of a metalloprotein active-site provides an opportunity to consider the function and associated mechanism of that metalloprotein at the molecular level. One nice example is the dinuclear cuprous amine-bis-pyridyl complex, which effects arene hydroxylation (albeit of the ligand m-xylyl spacer) using molecular oxygen (O2).1 This extraordinary reaction involves cleavage of the O-O bond and subsequent insertion of an oxygen atom into an arene C-H bond under essentially ambient conditions, to model the function of copper monooxygenases such as tyrosinase. Another excellent example is the generation of dicupric trans-µ-1,2-peroxo complexes from cuprous precursors and O2, reversibly,2–4 to model the oxygen-transport property of the protein hemocyanin, which subsequently was discovered to bind O2 in η2:η2 fashion, as shown in Figure 1.4 The metalloprotein cytochrome c oxidase,5 however, due to its combination of diverse and unusual active-site metal centers, has eluded a convincing model description. As for its function, it probably binds O2 at a dinuclear site comprising heme-iron and histidyl-copper coordination; it then cleaves the O-O bond, via reduction, (vide infra ).5 The structural changes associated with this dinuclear site during turnover, and the intermediates produced therefrom, are by no means clearly understood. In the resting state, the dinuclear site exhibits strong antiferromagnetic coupling (-J =200 cm-1) suggesting the involvement of a bridging ligand, often postulated as µ-sulfido, µ-chloro, or µ-hydroxo. Thus, we have endeavored to synthesize model complexes of this enigmatic dinuclear site.
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... 44, No. 6 A MOSSBAUER STUDY OF AMORPHOUS Fe40Ni40B20 909 3. B. Bhanu Prasad, AK Bhatnagar R. Jagannathan 17. Z. Marohnic, E. Babic, J. Ivkov A. Hamzic, Proc. ... (1976). 9. H. Franke, S. Dey, M. Rosenberg, FE Luborsky 24. RS Preston,... more
... 44, No. 6 A MOSSBAUER STUDY OF AMORPHOUS Fe40Ni40B20 909 3. B. Bhanu Prasad, AK Bhatnagar R. Jagannathan 17. Z. Marohnic, E. Babic, J. Ivkov A. Hamzic, Proc. ... (1976). 9. H. Franke, S. Dey, M. Rosenberg, FE Luborsky 24. RS Preston, SS Hanna J. Heberle, Phys. ...
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Abstract Ferrites of the formula BaCa1−xSrxFe4O8 (0 ⩽ x ⩽ 1) gave rise to magnetically split Mossbauer spectra indicative of antiferromagnetic ordering at room temperature. These spectra were analysed to yield the isomer-shift, quadrupole... more
Abstract Ferrites of the formula BaCa1−xSrxFe4O8 (0 ⩽ x ⩽ 1) gave rise to magnetically split Mossbauer spectra indicative of antiferromagnetic ordering at room temperature. These spectra were analysed to yield the isomer-shift, quadrupole splitting, internal magnetic field and its orientation. The unit cell dimensions were obtained from X-ray powder patterns and were used in obtaining estimates of the electric field gradient (e.f.g.). The calculated and observed e.f.g. values indicate increasing symmetry as x → 1. A temperature dependence study of BaCaFe4O8 gave a Neel temperature TN = 670 K and Heff(O) = 485 kOe.
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ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full... more
ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
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The synthesis of appropriate transition-metal complexes to model the structural, spectroscopic, and magnetic properties of a metalloprotein active-site provides an opportunity to consider the function and associated mechanism of that... more
The synthesis of appropriate transition-metal complexes to model the structural, spectroscopic, and magnetic properties of a metalloprotein active-site provides an opportunity to consider the function and associated mechanism of that metalloprotein at the molecular level. One nice example is the dinuclear cuprous amine-bis-pyridyl complex, which effects arene hydroxylation (albeit of the ligand m-xylyl spacer) using molecular oxygen (O2).1 This extraordinary reaction involves cleavage of the O-O bond and subsequent insertion of an oxygen atom into an arene C-H bond under essentially ambient conditions, to model the function of copper monooxygenases such as tyrosinase. Another excellent example is the generation of dicupric trans-µ-1,2-peroxo complexes from cuprous precursors and O2, reversibly,2–4 to model the oxygen-transport property of the protein hemocyanin, which subsequently was discovered to bind O2 in η2:η2 fashion, as shown in Figure 1.4 The metalloprotein cytochrome c oxidase,5 however, due to its combination of diverse and unusual active-site metal centers, has eluded a convincing model description. As for its function, it probably binds O2 at a dinuclear site comprising heme-iron and histidyl-copper coordination; it then cleaves the O-O bond, via reduction, (vide infra ).5 The structural changes associated with this dinuclear site during turnover, and the intermediates produced therefrom, are by no means clearly understood. In the resting state, the dinuclear site exhibits strong antiferromagnetic coupling (-J =200 cm-1) suggesting the involvement of a bridging ligand, often postulated as µ-sulfido, µ-chloro, or µ-hydroxo. Thus, we have endeavored to synthesize model complexes of this enigmatic dinuclear site.
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Hydrogen peroxide formed in cells, as the result of incomplete reduction of oxygen, can be removed essentially by two ways: by peroxidases in a process of reduction to water or by catalase in a dismutation reaction. The actions of these... more
Hydrogen peroxide formed in cells, as the result of incomplete reduction of oxygen, can be removed essentially by two ways: by peroxidases in a process of reduction to water or by catalase in a dismutation reaction. The actions of these enzymes are essential to prevent the accumulation of hydrogen peroxide, diminishing the risk of peroxide-induced damage of cell constituents [1].
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Abstract Ferrites of the formula BaCa1−xSrxFe4O8 (0 ⩽ x ⩽ 1) gave rise to magnetically split Mossbauer spectra indicative of antiferromagnetic ordering at room temperature. These spectra were analysed to yield the isomer-shift, quadrupole... more
Abstract Ferrites of the formula BaCa1−xSrxFe4O8 (0 ⩽ x ⩽ 1) gave rise to magnetically split Mossbauer spectra indicative of antiferromagnetic ordering at room temperature. These spectra were analysed to yield the isomer-shift, quadrupole splitting, internal magnetic field and its orientation. The unit cell dimensions were obtained from X-ray powder patterns and were used in obtaining estimates of the electric field gradient (e.f.g.). The calculated and observed e.f.g. values indicate increasing symmetry as x → 1. A temperature dependence study of BaCaFe4O8 gave a Neel temperature TN = 670 K and Heff(O) = 485 kOe.
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ABSTRACT The periplasmic hydrogenase of Desulfovibrio vulgaris (Hildenbourough NCIB 8303) belongs to the category of [Fe] hydrogenase which contains only iron-sulfur clusters as its prosthetic groups. Amino acid analyses were performed on... more
ABSTRACT The periplasmic hydrogenase of Desulfovibrio vulgaris (Hildenbourough NCIB 8303) belongs to the category of [Fe] hydrogenase which contains only iron-sulfur clusters as its prosthetic groups. Amino acid analyses were performed on the purified D. vulgaris hydrogenase. The amino acid composition obtained compared very well with the result derived from the nucleotide sequence of the structural gene (Voordouw, G., Brenner, S. (1985) Eur. J. Biochem. 148, 515-520). Detailed EPR reductive titration studies on the D. vulgaris hydrogenase were performed to characterize the metal centers in this hydrogenase. In addition to the three previously observed EPR signals (namely, the "isotropic" 2.02 signal, the rhombic 2.10 signal, and the complex signal of the reduced enzyme), a rhombic signal with resonances at the g-values of 2.06, 1.96, and 1.89 (the rhombic 2.06 signal) was detected when the samples were poised at potentials between 0 and -250 mV (with respect to normal hydrogen electrode). The midpoint redox potentials for each of the four EPR-active species were determined, and the characteristics of each EPR signal are described. Both the rhombic 2.10 and 2.06 signals exhibit spectral properties that are distinct from a ferredoxin-type [4Fe-4S] cluster and are proposed to originate from the same H2-binding center but in two different conformations. The complex signal of the reduced hydrogenase has been shown to represent two spin-spin interacting ferredoxin-type [4Fe-4S]1+ clusters (Grande, H. J., Dunham, W. R., Averill, B., Van Dijk, C., and Sands, R. H. (1983) Eur. J. Biochem. 136, 201-207). The titration data indicated a strong cooperative effect between these two clusters during their reduction. In an effort to accurately estimate the number of iron atoms/molecule of hydrogenase, plasma emission and chemical methods were used to determine the iron contents in the samples; and four different methods, including amino acid analysis, were used for protein determination. The resulting iron stoichiometries were found to be method-dependent and vary over a wide range (+/- 20%). The uncertainties involved in the determination of iron stoichiometry are discussed.
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Metallic glass Fe 72 Co 3 Si 15 B 10 has been investigated using Mossbauer spectroscopy, electrical resistivity and thermoelectric power techniques. The saturation hyperfine magnetic field H eff (0), Curie temperature, T c and... more
Metallic glass Fe 72 Co 3 Si 15 B 10 has been investigated using Mossbauer spectroscopy, electrical resistivity and thermoelectric power techniques. The saturation hyperfine magnetic field H eff (0), Curie temperature, T c and crystallization temperature, T x for the sample are found to be 265 ± 5 kOe, 725 ± 5 K and 810 ± 5 K, respectively, by the Mossbauer spectroscopy. Reduced hyperfine magnetic fields vs. reduced temperatures show a similar departure from the Brillouin curve as observed for other iron-rich metallic glasses and can be fitted to the Handrich's model with some modification. Distribution of hyperfine magnetic fields has been evaluated at room temperature which consists of a major single peak centred around the magnetic field close to the measured value of average hyperfine magnetic field H eff . Electrical resistivity data show that the crystallization takes place in two-step process with primary crystallization setting in at 815 K. Absolute thermoelectric power S of the sample is found to be negative through out the temperature region 80 K — 800 K and shows a parabolic behaviour with a minimum around 310 K with S= −5.6 μV/K Value of S falls steeply on crystallization.
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X-ray Structure and Physical Properties of the Oxo-Bridged ... Complex [(Fg-TPP)Fe-O-Cu(TMPA )]+, F8-TPP = ... Tris( 2-pyridylmethy1)amine: Modeling the Cytochrome c ... Kenneth D. Karlin,*vt Alaganandan Nanthakumar,+ Stephen Fox,t... more
X-ray Structure and Physical Properties of the Oxo-Bridged ... Complex [(Fg-TPP)Fe-O-Cu(TMPA )]+, F8-TPP = ... Tris( 2-pyridylmethy1)amine: Modeling the Cytochrome c ... Kenneth D. Karlin,*vt Alaganandan Nanthakumar,+ Stephen Fox,t Narasimha N. Murthy,? Natarajan ...
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Alloys ZrCrFe_0.5Co_0.5 and ZrMnFe_0.5Ni_0.5 are efficient in absorbing hydrogen into the interstitial positions of the C14 hexagonal lattice and are promising materials as an alternate source of hydrogen. The room temperature ^57Fe... more
Alloys ZrCrFe_0.5Co_0.5 and ZrMnFe_0.5Ni_0.5 are efficient in absorbing hydrogen into the interstitial positions of the C14 hexagonal lattice and are promising materials as an alternate source of hydrogen. The room temperature ^57Fe Mössbauer spectra of ZrCrFe_0.5Co_0.5 and its hydrides consists of a quadrupole doublet with a very small splitting. The parent system shows an apparent isomer-shift (delta) of -0.20(0.04) mm/s
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The Zr based AB2 alloys ZrMnFe0.5Ni0.5, ZrMnFe0.5Co0.5 and mischmetal (Mm) based AB5 alloy MmNi3.5Al0.5Fe0.5Co0.5 have been prepared and characterized by means of powder x-ray diffractograms. The hydrogen absorption kinetics of these... more
The Zr based AB2 alloys ZrMnFe0.5Ni0.5, ZrMnFe0.5Co0.5 and mischmetal (Mm) based AB5 alloy MmNi3.5Al0.5Fe0.5Co0.5 have been prepared and characterized by means of powder x-ray diffractograms. The hydrogen absorption kinetics of these alloys have been studied in the temperature and pressure ranges 450-650 °C and 10-100 mbar respectively with a maximum H to host alloy formula unit ratio of 0.01, using
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... Natarajan Ravi,t Benet C. Prickril,i.ll Donald M. Kurtz, Jr.,*ss and Boi Hanh Huynh'J Department of Physics, Emory University, Atlanta, Georgia 30322, and Department of Chemistry and Center for Metalloenzyme Studies,... more
... Natarajan Ravi,t Benet C. Prickril,i.ll Donald M. Kurtz, Jr.,*ss and Boi Hanh Huynh'J Department of Physics, Emory University, Atlanta, Georgia 30322, and Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602 Received ...
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ABSTRACT
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Ferrites and perovskites, two major classes of ceramic compounds, exhibit electrical and magnetic properties that make them suitable for a wide variety of technological applications. A study of such systems has been initiated in our... more
Ferrites and perovskites, two major classes of ceramic compounds, exhibit electrical and magnetic properties that make them suitable for a wide variety of technological applications. A study of such systems has been initiated in our laboratory with the ultimate objective of making nanoscale materials. Antiferromagnetic solid solutions, CaBaFe_4(1-x)Al_4xO8 (0<x<0.5), have been prepared by conventional high-temperature ceramic techniques and characterized by
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ABSTRACT
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The VFe protein of alternative nitrogenase, isolated from Azotobacter vinelandii, strain LS15 and designated as Av1', has been investigated by Mössbauer spectroscopy. The Mössbauer spectrum of the dithionite-reduced Av1', recorded... more
The VFe protein of alternative nitrogenase, isolated from Azotobacter vinelandii, strain LS15 and designated as Av1', has been investigated by Mössbauer spectroscopy. The Mössbauer spectrum of the dithionite-reduced Av1', recorded at 4.2 K with a 60-millitesla magnetic field applied parallel to the gamma-beam, is a superposition of three spectral components: 1) a complex spectrum (the M component) with magnetic hyperfine structures attributed to the paramagnetic FeV cofactor, 2) a component (the P component) consisting of three quadrupole doublets identifiable as the Fe2+, D, and S doublets similar to those observed for the P cluster pairs in MoFe proteins, and 3) a minor (4% of total absorption) quadrupole doublet attributable to adventitiously bound iron. The observed 4.2-K parameters for the Fe2+ (delta EQ = 2.99 mm/s and delta = 0.64 mm/s), D (delta EQ = 0.75 mm/s and delta = 0.63 mm/s), and S (delta EQ = 1.2 mm/s and delta = 0.65 mm/s) iron sites and their temperature d...
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The SF-Abs, RFQ-EPR, and RFQ-Möss data on the R2 reconstitution reaction are all consistent with the mechanism of Scheme I, in which the intermediate X is the immediate precursor to the product cofactor, and illustrate how the continuous... more
The SF-Abs, RFQ-EPR, and RFQ-Möss data on the R2 reconstitution reaction are all consistent with the mechanism of Scheme I, in which the intermediate X is the immediate precursor to the product cofactor, and illustrate how the continuous SF approach and the discontinuous RFQ methods can be complementary. Given the inherent differences in the methods, it should not be taken for granted that data from the two will be consistent. A number of problems can be associated with the RFQ approach. For example, isopentane could conceivably interfere with or alter the chemistry to be studied. A second potential problem involves temperature-dependent equilibria among different intermediate species. This problem has been encountered by Dooley et al. with the 6-hydroxydopa-requiring protein, plasma amine oxidase and was previously observed with the adenosylcobalamin-dependent ribonucleotide reductase by Blakley and co-workers. This potential complication should be considered when discrepancies ari...
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Recent experimental work has demonstrated production of quasi-free-standing graphene by methane intercalation. The intercalation weakens the coupling of adjacent graphene layers and yields Dirac fermion behaviour of monolayer graphene. We... more
Recent experimental work has demonstrated production of quasi-free-standing graphene by methane intercalation. The intercalation weakens the coupling of adjacent graphene layers and yields Dirac fermion behaviour of monolayer graphene. We have investigated the electronic characteristics of a methane intercepted graphene bilayer under a perpendicularly applied electric field. Evolution of the band structure of intercalated graphene as a function of the bias is studied by means of density-functional theory including interlayer van der Waals interactions. The implications of controllable band gap opening in methane-intercalated graphene for future device applications are discussed.
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X-ray Structure and Physical Properties of the Oxo-Bridged ... Complex [(Fg-TPP)Fe-O-Cu(TMPA )]+, F8-TPP = ... Tris( 2-pyridylmethy1)amine: Modeling the Cytochrome c ... Kenneth D. Karlin,*vt Alaganandan Nanthakumar,+ Stephen Fox,t... more
X-ray Structure and Physical Properties of the Oxo-Bridged ... Complex [(Fg-TPP)Fe-O-Cu(TMPA )]+, F8-TPP = ... Tris( 2-pyridylmethy1)amine: Modeling the Cytochrome c ... Kenneth D. Karlin,*vt Alaganandan Nanthakumar,+ Stephen Fox,t Narasimha N. Murthy,? Natarajan ...
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... iron(III)-Copper(I1) Species as Cytochrome c Oxidase Models: Acid-Base Interconversions and X ... 0.1 p~g (solution, Evans method in CHzC12), compared to 5.1 f 0.1 p~g (both ... clear relationship between 3 and 4 is revealed by their... more
... iron(III)-Copper(I1) Species as Cytochrome c Oxidase Models: Acid-Base Interconversions and X ... 0.1 p~g (solution, Evans method in CHzC12), compared to 5.1 f 0.1 p~g (both ... clear relationship between 3 and 4 is revealed by their reversible acid-base interconversion, Scheme I ...