Hα Emission as a feedback control sensor for reactive sputter deposition of nano-structured, diamond-like carbon coatings
C. Christopher Klepper, Eric P. Carlson, Robert C. Hazelton, Edward J. Yadlowsky, Bao Feng, Mahmoud A. Taher, and Harry M. Meyer, III
Abstract
This paper discusses the potential use of the hydrogen atomic line emission at 656.3 nm (Hα ) as an effective in-situ sensor for a closed-loop control system to improve the reproducibility of reactive sputter deposition of nano-structured, metal-containing, hydrogenated, diamond-like carbon (Me:DLC:H) coatings. The paper includes experimental results showing a good correlation between Hα emission in the process plasma and the formation of metal-carbide, an important component of these coatings. The first attempts at actual feedback-control of the process showed that this sensor can be effective, at least over the stage of the deposition when mostly carbides are formed in the coating. A spectrally resolved analysis of the Hα emission for the various stages of the deposition have shown that the emission profile is dominated by a “hot” component ( ~10–20 eV), which can be attributed to dissociative excitation of molecular hydrogen (H2). The molecular hydrogen is understood to evolve from the coating as a result of carbon incorporation from the reactive gas (C2H2) and is particularly sensitive to metal carbide formation in the film, when most of the hydrogen is released from the surface in molecular form.
IEEE TRANSACTIONS ON PLASMA SCIENCE, VOL. 33, NO. 2, APRIL 2005
Resonance Raman study of the phonon spectra in superconducting Bi-2212 and Y-123
M. Rübhausenb , M.V. Kleina, D. Budelmannb, B. Schulzb, P. Guptasarmac, M.S. Williamsenc, R. Liangd, D.A. Bonnd and W.N. Hardyd
Abstract
We studied the variation of phonon spectra with incident photon energy Ei in two superconducting samples, optimally doped YBCO (Tc=93.6 K) and overdoped Bi-2212 (Tc=82 K). Our results highlight the layered nature of the cuprates. Especially the buffer layers that are thought to be responsible for the doping of the CuO2 planes show complex phonon spectra. In Bi-2212 we find an activation of up to 13 phonon modes for a resonance that allows transitions into the Bi–O layers at 3.8 eV. For Y-123 we find also an activation of phonon modes as well as a huge matrix element when transitions into the chains at around 4.1 eV are possible. We also investigate the variation of the line shape of the O(II)–O(III) mode as a function of incident photon energy.
Journal of Physics and Chemistry of Solids 2006, Volume 67, Issues 1-3, Pages 312-315
Fully reflective deep ultraviolet to near infrared spectrometer and entrance optics for resonance Raman spectroscopy
B. Schulz, J. Bäckström, D. Budelmann, R. Maeser, M. Rübhausen, M. V. Klein, E. Schoeffel, A. Mihill and S. Yoon
Abstract
We present the design and performance of a new triple-grating deep ultraviolet to near-infrared spectrometer. The system is fully achromatic due to the use of reflective optics. The minimization of image aberrations by using on- and off- axis parabolic mirrors as well as elliptical mirrors yields a strong stray light rejection with high resolution over a wavelength range between 165 and 1000 nm. The Raman signal is collected with a reflective entrance objective with a numerical aperture of 0.5, featuring a Cassegrain-type design. Resonance Raman studies on semiconductors and on correlated compounds, such as LaMnO3, highlight the performance of this instrument, and show diverse resonance effects between 1.96 and 5.4 eV
Review of scientific instruments
2005, Volume 76, no7, pp. 073107.1-073107.12
Orbital ordering in LaMnO3 investigated by resonance Raman spectroscopy
Krüger R, Schulz B, Naler S, Rauer R, Budelmann D, Bäckström J, Kim KH, Cheong SW, Perebeinos V, Rübhausen M.
Abstract
Orbital ordering leads to an unconventional excitation spectrum that we investigate by resonance Raman scattering using incident photon energies between 1.7 and 5.0 eV. We use spectral ellipsometry to determine the corresponding dielectric function. Our results show resonant behavior of the phonon Raman cross section when the laser frequency is close to the orbiton-excitation energy of 2 eV in LaMnO3. We show an excellent agreement between theoretical calculations based on the Franck-Condon mechanism activating multiphonon Raman scattering in first order of the electron-phonon coupling and the experimental data of phonons with different symmetries.
Physical Review Letters, vol. 92, Issue 9, id. 097203
Primary realization of a spectral irradiance scale employing monochromator-based cryogenic radiometry between 200 nm and 20 µm
E W M van der Ham, H C D Bos and C A Schrama
Abstract
Here we report on an alternative approach for making spectral irradiance measurements of radiation sources traceable, employing our monochromator-based absolute cryogenic radiometer (ACR) facility to its full extent. The method makes use of the continuously tunable absolute radiant flux emerging from the ACR facility to characterize and calibrate the spectral irradiance responsivity of a second adjacent double-monochromator system. This system will be part of a new facility at NMi-VSL, called SIR, that will be used to measure spectral irradiance distributions of radiation sources from the ultraviolet to the far infrared. Following this traceability route, a fully characterized high-temperature Planckian radiator is not needed. Proof-of-principle measurements in the visible part of the spectrum show very encouraging results. Although the new facility is under construction, the theoretical background and a schematic description will be presented in this paper.
2003 Metrologia 40 S177-S180
Picosecond relaxation of Ni-centers in II–VI semiconductors
R. Heitz, A. Hoffmann and I. Broser
Abstract
The internal relaxation processes of the 3d-center Ni2+ and the recombination of photogenerated holes with Ni+-centers are investigated by means of time resolved luminescence spectroscopy of the 3T1(P)-3T1(F) Ni2+ transition in ZnS, CdS, ZnSe and CdSe. Ultrafast recombination processes starting at the 3T1(P)-states with time constants down to 60 ps are observed. In addition to the detected dipole transitions, which are allowed by a strong admixture of p-like wavefunctions to the 3d-states of Ni2+, competing nonradiative recombination processes are important. Radiative and nonradiative transition rates are determined. The excitation processes of the 3T1(P)-3T1(F) luminescence are studied in cw and time resolved experiments. Free holes are trapped at Ni+-centers forming shallow effective mass-like states, trapping times of 30 ps in ZnS and 50 ps in CdS are observed. The subsequent intracenter relaxation to the luminescent 3T1(P)-state takes place within a few picoseconds by radiotionless cascade processes involving the 1T2(G)-state. After some nanoseconds the dynamical behaviour of the Ni2+-luminescence is determined by energy transfer processes between shallow donors and the Ni2+-centers. The investigations give evidence of strong electronic coupling of the Ni2+ (d-d)-transitions to the host
Optical Materials I 1992, 75-83
Picosecond energy transfer between excitons and defects in II-IV semiconductors
R.Heitz, C.Fricke, A.Hoffmann and I.Broser
Abstract
The luminescences of bound excitons in various II-IV semiconductors are studied by means of
time resolved spectroscopy at liquid helium temperatures. A general trend of increasing lifetimes
with increasing binding energies is in reasonable agreement with the theory of Rashba and
Gurgenishvili indicating a predominant radiative decay. It is shown that the investigation of the
dynamics of weakly bound excitons provides the possibility to determine parameters of the free
exciton. An effective exciton mass of 1.06m0 for ZnO and a free excitan oscillator strength of
0.0014 for ZnS are determined. The limits of the model in case of deeply bound excitons as well
as the nonradiative decay channels are discussed. The observed luminescence risetimes due to
the formation of bound exciton complexes after generation of free excitons are investigated.
Materials Science Forum Vol. 83-87 (1992) pp. 1241-1246
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Thermal Dependence of the Cr-to-Nd Energy Transfer in Lanthanum Lutetium Gallium Garnet
G. Ozen and B. Dibartolo
Abstract
Photoluminescence, excitation, and response to pulsed excitation measurements show the existence of the Cr3+-to-Nd3+ energy transfer in lanthanum lutetium gallium garnet with an efficiency eta = 0.59 at room temperature. The transfer occurs radiatively and nonradiatively, and both transfer rates are temperature dependent within 15-550 K. The nonradiative transfer rate, calculated as a function of temperature by using the lifetime data of the Cr3+ ion in the crystal, increases slowly with increasing temperature.
Applied Spectroscopy, Vol. 53, Issue 11, pp. 1454-1458
Red Antenna States of Photosystem I from Cyanobacteria Synechocystis PCC 6803 and Thermosynechococcus elongatus: Single-Complex Spectroscopy and Spectral Hole-Burning Study
Kerry J. Riley, Tőnu Reinot, Ryszard Jankowiak, Petra Fromme, and Valter Zazubovich
Abstract
Hole-burning and single photosynthetic complex spectroscopy were used to study the excitonic structure and excitation energy-transfer processes of cyanobacterial trimeric Photosystem I (PS I) complexes from Synechocystis PCC 6803 and Thermosynechococcus elongatus at low temperatures. It was shown that individual PS I complexes of Synechocystis PCC 6803 (which have two red antenna states, i.e., C706 and C714) reveal only a broad structureless fluorescence band with a maximum near 720 nm, indicating strong electron-phonon coupling for the lowest energy C714 red state. The absence of zero-phonon lines (ZPLs) belonging to the C706 red state in the emission spectra of individual PS I complexes from Synechocystis PCC 6803 suggests that the C706 and C714 red antenna states of Synechocystis PCC 6803 are connected by efficient energy transfer with a characteristic transfer time of 5 ps. This finding is in agreement with spectral hole-burning data obtained for bulk samples of Synechocystis PCC 6803. The importance of comparing the results of ensemble (spectral hole burning) and single-complex measurements was demonstrated. The presence of narrow ZPLs near 710 nm in addition to the broad fluorescence band at 730 nm in Thermosynechococcus elongatus (Jelezko et al. J. Phys. Chem. B 2000, 104, 8093-8096) has been confirmed. We also demonstrate that high-quality samples obtained by dissolving crystals of PS I of Thermosynechococcus elongatus exhibit stronger absorption in the red antenna region than any samples studied so far by us and other groups.
J. Phys. Chem. B, 2007, 111 (1), pp 286–292
Biophysical and Structural Analysis of a Novel Heme b Iron Ligation in the Flavocytochrome Cellobiose Dehydrogenase
Frederik A. J. Rotsaert, B. Martin Hallberg, Simon de Vries, Pierre Moenne-Loccoz, Christina Divne, V. Renganathan and Michael H. Gold
Abstract
The fungal extracellular flavocytochrome cellobiose dehydrogenase (CDH)
participates in lignocellulose degradation. The enzyme has a cytochrome domain
connected to a flavin-binding domain by a peptide linker. The cytochrome
domain contains a 6-coordinate low spin b-type heme with unusual iron
ligands and coordination geometry. Wild type CDH is only the second example of
a b-type heme with Met-His ligation, and it is the first example of a
Met-His ligation of heme b where the ligands are arranged in a nearly
perpendicular orientation. To investigate the ligation further,
Met65 was replaced with a histidine to create a
bis-histidyl ligated iron typical of b-type cytochromes. The
variant is expressed as a stable 90-kDa protein that retains the flavin domain
catalytic reactivity. However, the ability of the mutant to reduce external
one-electron acceptors such as cytochrome c is impaired.
Electrochemical measurements demonstrate a decrease in the redox midpoint
potential of the heme by 210 mV. In contrast to the wild type enzyme, the
ferric state of the protoheme displays a mixed low spin/high spin state at
room temperature and low spin character at 90 K, as determined by resonance
Raman spectroscopy. The wild type cytochrome does not bind CO, but the ferrous
state of the variant forms a CO complex, although the association rate is very
low. The crystal structure of the M65H cytochrome domain has been determined
at 1.9 Å resolution. The variant structure confirms a
bis-histidyl ligation but reveals unusual features. As for the wild
type enzyme, the ligands have a nearly perpendicular arrangement. Furthermore,
the iron is bound by imidazole Nδ1 and Nε2 nitrogen atoms, rather than the typical Nε2 /Nε2 coordination encountered in bis-histidyl ligated heme proteins. To our knowledge, this is the first example of a bis-histidyl Nδ1 /Nε2 -coordinated protoporphyrin IX iron.
Journal of Physics and Chemistry of Solids
Volume 67, Issues 1-3, January-March 2006, Pages 312-315
Peroxodiferric Intermediate of Stearoyl-Acyl Carrier Protein Δ9 Desaturase: Oxidase Reactivity during Single Turnover and Implications for the Mechanism of Desaturation
John A. Broadwater, Jingyuan Ai, Thomas M. Loehr,Joann Sanders-Loehr, and Brian G. Fox
Abstract
Combined optical and resonance Raman studies have revealed the formation of an O2-adduct upon exposure of 4e- chemically reduced stearoyl-acyl carrier protein Δ9 desaturase to stearoyl-ACP and 1 atm O2. The observed intermediate has a broad absorption band at 700 nm and is remarkably stable at room temperature (t1/2≈26 min). Resonance Raman studies using 16O2 gas reveal vibrational features of a bound peroxide [vs(Fe-O2), 442 cm-1; vas(Fe-O2), 490 cm-1; v(O-O), 898 cm-1] that undergo the expected mass-dependent shifts when prepared in 16O18O or 18O2. The appearance of two Fe-O2 vibrations, each having a single peak of intermediate frequency with 16O18O, proves that the peroxide is bound symmetrically between the two iron atoms in a µ-1,2 configuration. The same results have been obtained in the accompanying resonance Raman study of ribonucleotide reductase isoform W48F/D84E [P. Moënne-Loccoz, J. Baldwin, B. A. Ley, T. M. Loehr, and J. M. Bollinger, Jr. (1998) Biochemistry 37, 14659-14663], thus making it likely that other members of the class II diiron enzymes form related peroxodiferric intermediates. Study of the reactivity of peroxodiferric δ9D revealed that this intermediate underwent 2e- reduction leading to an oxidase reaction and recovery of the resting ferric homodimer. In contrast, biological reduction of the same enzyme preparations using ferredoxin reductase and [2Fe-2S] ferredoxin gave catalytic desaturation with a turnover number of 20-30 min-1. The profound difference in catalytic outcome for chemically and enzymatically reduced Δ9D suggests that redox-state dependent conformational changes cause partition of reactivity between desaturase and oxidase chemistries. The Δ9D oxidase reaction represents a new type of reactivity for the acyl-ACP desaturases and provides a two-step catalytic precedent for the “alternative oxidase” activity recently proposed for a membrane diiron enzyme in plants and trypanosomes.
Biochemistry, 1998, 37 (42), pp 14664–14671
The Ferroxidase Reaction of Ferritin Reveals a Diferric µ-1,2 Bridging Peroxide Intermediate in Common with Other O2-Activating Non-Heme Diiron Proteins
Pierre Moënne-Loccoz, Carsten Krebs, Kara Herlihy, Dale E. Edmondson, Elizabeth C. Theil, Boi Hanh Huynh, and Thomas M. Loehr
Abstract
Ferritins are ubiquitous proteins that concentrate, store, and detoxify intracellular iron through oxidation of Fe2+ (ferroxidation), followed by translocation and hydrolysis to form a large inorganic mineral core. A series of mutagenesis, kinetics, and spectroscopic studies of ferritin led to the proposal that the oxidation/translocation path involves a diiron protein site. Recent stopped-flow absorption and rapid freeze-quench Mössbauer studies have identified a single peroxodiferric species as the initial transient intermediate formed in recombinant frog M ferritin during rapid ferroxidation [Pereira, S. A., Small, W., Krebs, C., Tavares, P., Edmondson, D. E., Theil, E. C., and Huynh, B. H. (1998) Biochemistry 37, 9871-9876]. To further characterize this transient intermediate and to establish unambiguously the peroxodiferric assignment, rapid freeze-quenching was used to trap the initial intermediate for resonance Raman investigation. Discrete vibrational modes are observed for this intermediate, indicating a single chromophore in a homogeneous state, in agreement with the Mössbauer conclusions. The frequency at 851 cm-1 is assigned as v(O-O) of the bound peroxide, and the pair of frequencies at 485 and 499 cm-1 is attributed, respectively, to vs and vas of Fe-O2-Fe. Identification of the chromophore as a µ-1,2 bridged diferric peroxide is provided by the isotope sensitivity of these Raman bands. Similar peroxodiferric intermediates have been detected in a mutant of the R2 subunit of ribonucleotide reductase from Escherichia coli and chemically reduced Δ9 stearoyl-acyl carrier protein desaturase (Δ9D), but in contrast, the ferritin intermediate is trapped from the true reaction pathway of the native protein. Differences in the Raman signatures of these peroxide species are assigned to variations in Fe-O-O-Fe angles and may relate to whether the iron is retained in the catalytic center or released as an oxidized product.
Biochemistry, 1999, 38 (17), pp 5290–5295
Visible spectroscopy measurements in the PBFA II ion diode (invited)
J. Bailey, A. L. Carlson, R. L. Morrison and Y. Maron
Abstract
We describe a new visible spectroscopy diagnostic system for measuring plasma properties in the PBFA II applied-B ion diode. The system transports light from the ion diode to a remote screen room where it is recorded by a spectrograph coupled to a streak camera. We developed extensive calibration techniques for measuring the collection efficiency into the fiber link, the effects of the background bremsstrahlung radiation on the fibers, the fiber transmission as a function of wavelength, and the absolute streaked-spectrograph sensitivity as a function of wavelength. We have recorded time-dependent spectral line profiles and intensities from the PBFA II plasma opening switch, the beam-transport gas cell, and the anode plasma. The Stark shift of the LiI 2s-2p transition observed on LiF-anode shots shows that the time-resolved electric field peaks at 7–8 MV/cm, the highest field ever measured using the Stark effect. The potential of these measurements to expand our knowledge of ion-diode physics is being explored. Review of Scientific Instruments is copyrighted by The American Institute of Physics.
Rev. Sci. Instrum. 61, 3075 (1990); doi:10.1063/1.1141686
Biosynthesis of topa quinone cofactor in bacterial amine oxidases. Solvent origin of C-2 oxygen determined by Raman spectroscopy.
Nakamura N, Matsuzaki R, Choi YH, Tanizawa K, Sanders-Loehr J.
Abstract
Resonance Raman spectroscopy is an excellent technique for providing structural information on the 2,4, 5-trihydroxyphenylalanine quinone (TPQ) cofactor in copper-containing amine oxidases. This technique has been used to investigate the copper- and O2-dependent biosynthesis of the TPQ cofactor in phenylethylamine oxidase (PEAO) and histamine oxidase from Arthrobacter globiformis. Incubation of the holoenzyme in H218O causes frequency shifts at 1684(-26) cm-1 in PEAO and at 1679(-28) cm-1 in histamine oxidase, allowing this feature to be assigned to the C=O stretch of a single carbonyl group at the C-5 position. When apoprotein is reacted with Cu(II) and O2 in the presence of H218O, the resultant holoproteins show increased shifts of -3 to -6 cm-1 in a number of other vibrational modes, particularly at 411 and 1397 cm-1. Because these small shifts persist when the H218O-regenerated protein is back-exchanged into H216O, they can be assigned to oxygen isotope substitution at the C-2 postion. No isotope shifts are observed when apoprotein is regenerated with Cu(II) in the presence of 18O2. Thus, it is concluded that the C-2 oxygen atom of TPQ originates from H2O rather than O2. The isotope dependence of the 1397-cm-1 mode allows it to be assigned to the C-O moiety at the C-2 position, with its low frequency being indicative of only partial double bond character. Similar frequency shifts due to 18O at C-2 are observed in the resonance Raman spectra of H218O-regenerated PEAO after derivatization of the C-5 carbonyl with either p-nitrophenylhydrazine (-5 cm-1 at 480 cm-1) or methylamine (-5 cm-1 at 1301 cm-1). Taken together, these results indicate that the TPQ cofactor in the native enzyme has substantial electron delocalization between the C-2 and C-4 oxygens and that only the C-5 oxygen has predominantly C=O character.
J Biol Chem. 1996 Mar 1;271(9):4718-24.
Characterization of Manganese(II) Binding Site Mutants of Manganese Peroxidase
Katsuyuki Kishi, Margo Kusters-van Someren,‡ Mary B. Mayfield, Jie Sun, Thomas M. Loehr, and Michael H. Gold*
Abstract
A series of site-directed mutants, E35Q, E39Q, and E35Q-D179N, in the gene encoding manganese peroxidase isozyme 1 (mnp1) from Phanerochaete chrysosporium, was created by overlap extension, using the polymerase chain reaction. The mutant genes were expressed in P. chrysosporium during primary metabolic growth under the control of the glyceraldehyde-3-phosphate dehydrogenase promoter. The mutant manganese peroxidases (MnPs) were purified and characterized. The molecular masses of the mutant proteins, as well as UV-vis spectral features of their oxidized states, were very similar to those of the wild-type enzyme. Resonance Raman spectral results indicated that the heme environment of the mutant MnP proteins also was similar to that of the wild-type protein. Steady-state kinetic analyses of the E35Q and E39Q mutant MnPs yielded Km values for the substrate MnII that were ∼50-fold greater than the corresponding Km value for the wild-type enzyme. Likewise, the kcat values for MnII oxidation were ∼300-fold lower than that for wild-type MnP. With the E35Q-D179N double mutant, the Km value for MnII was ∼120-fold greater, and the kcat value was ∼1000-fold less than that for the wild-type MnP1. Transient-state kinetic analysis of the reduction of MnP compound II by MnII allowed the determination of the equilibrium dissociation constants (KD) and first-order rate constants for the mutant proteins. The KD values were approximately 100-fold higher for the single mutants and approximately 200-fold higher for the double mutant, as compared with the wild-type enzyme. The first-order rate constants for the single and double mutants were ∼200-fold and ∼4000-fold less, respectively, than that of the wild-type enzyme. In contrast, the Km values for H2O2 and the rates of compound I formation were similar for the mutant and wild-type MnPs. The second-order rate constants for p-cresol and ferrocyanide reduction of the mutant compounds II also were similar to those of the wild-type enzyme.
Biochemistry, 1996, 35 (27), pp 8986–8994
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