Determination of quenching coefficients in a hydrogen RF discharge by time-resolved optical emission spectroscopy

In gas discharges at elevated pressure, radiation-less collisional de-excitation (quenching) has a strong influence on the population of excited states. The knowledge of quenching coefficients is therefore important for plasma diagnostics and simulations. A novel time-resolved optical emission spectroscopic (OES) technique allows the measurement of quenching coefficients for emission lines of various species, particularly of noble gases, with molecular hydrogen as collision partner. The technique exploits the short electron impact excitation during the field reversal phase within the sheath region of a hydrogen capacitively coupled RF discharge at 13.56 MHz. Quenching coefficients can be determined subsequent to this excitation from the effective lifetime of the fluorescence decay at various hydrogen pressures. The measured quenching coefficients agree very well with results obtained by means of laser excitation. The time-resolved OES technique based on electron impact excitation is not limited - in contrast to laser techniques - by optical selection rules and the energy gap between the ground state and the observed excited level.

TIME-RESOLVED RESONANCE RAMAN-SPECTROSCOPY OF TRIPLET-STATE METALATED AND FREE-BASE TETRAARYLPORPHYRINS

Resonance Raman spectra of the T-1 excited states of Zn and free-base tetra-4-sulfonatophenylporphyrin (TPPS) have been recorded at room temperature in aqueous solution using two-colour time-resolved methods. The spectra of both sulfonated molecules are very similar to their tetraphenylporphyrin (TPP) analogues, which have been recorded in THF solution using the same pump-probe conditions, but they have higher signal-to-noise ratios because interference from strong solvent bands is reduced. Although two different T-1 spectra of Zn(TPP) have been reported these spectra differ slightly from each other and from the spectrum reported here, which has band positions very close (+/-6 cm(-1)) to those of Zn(TPPS). The high S/N ratios obtainable for the water-soluble porphyrins have allowed reliable polarization data to be recorded for their S-0 and T-1 states. This data set allows a realistic comparison of the changes in bonding associated with excitation of both free-base and Zn tetraarylporphyrins to the T-1 state.

TIME-RESOLVED RESONANCE RAMAN-SPECTROSCOPY OF EXCITED SINGLET AND TRIPLET-STATES OF FREE-BASE MESO-TETRAPHENYLPORPHYRIN

Two-color time-resolved resonance Raman spectroscopy has been used to probe the lowest excited singlet (S1) and triplet (T1) states of free-base meso-tetraphenylporphyrin and meso-tetrakis(4-sulphonatophenyl)porphyrin in solution at room temperature. The spectra were recorded using 532-nm excitation pulses and time-delayed probe pulses (DELTAT = 0-30 ns, 447 and 460 nm) near lambda(max) of the S1 and T1 states. Significant shifts in frequency of the porphyrin core vibrations were observed upon excitation to either the S1 or T1 state. Several of the strongest polarized bands in the spectra of both excited states, including nu1, nu2, nu4, nu6, and phi4, are assigned, and the information they give on the differences in electron distribution in the ground, S1, and T1 states is discussed.

A time-resolved spectroscopy study of the resonance-line emission in the Ge XXIII XUV laser

A comparison is presented of the temporally resolved resonance-line emission from the Ne-like Ge XUV laser (pumped with nanosecond pulses) with the predictions for the same emission from the hydro-atomic code EHYBRID. The specific lines chosen were the two 3s-2p Ne-like lines at 10.01 and 9.762 Angstrom, and the 3s-2p F-like group of lines in the 9.4-9.6 Angstrom region. Modification of the code to include 112 excited levels of the F-like ion facilitated a direct comparison between experiment and model of (i) the temporal variation of the emissions and (ii) the variation of the peak intensity ratios of the F-like to Ne-like emissions with irradiance on target.

Time-Resolved DRIFTS, MS, and Resistance Study of SnO2 Materials: The Role of Surface Hydroxyl Groups in Formation of Donor States

Time-resolved DRIFTS, MS, and resistance measurements were used to study the interaction of undoped and Pd-doped SnO2 with H-2 in air and argon at 300 degrees C. Using first-order kinetics, we compare the time constants for the resistance drop and its partial recovery with those of the surface hydroxyl evolution and water formation in the gas phase upon exposure to hydrogen. In the case of the undoped oxide, resistance and bridging hydroxyls (BOHs) evolve similarly, manifesting a fast main drop followed by recovery at a similar rate. The rate of water formation for this material was found to be much slower than that of the main drop in both the resistance and BOHs. In contrast, the resistance change for SnO2-Pd appeared to be similar to that of water formation, and no correlation was found between the evolution of resistance and surface OHs. Isotopic exchange on both materials revealed that water formation occurs via fast and slow hydrogen transfer to surface oxygen species. While the former originates from just-adsorbed hydrogen, the latter appears to proceed from the preadsorbed OHs. Both surfaces exhibit close interaction between chemisorbed oxygen and existing bridging OH groups, indicating that the latter is an intermediate in the hydrogen oxidation and generation of donor states on the surface.

A time-resolved electron paramagnetic resonance spectroscopy study of paramagnetic porphyrins /

There is considerable interest in intramolecular energy transfer, especially in complexes which absorb visible light, because it is crucial to the better understanding of photoharvesting systems in photosynthetic organisms and for utilizing solar energy as well. Porphyrin dimers represent one of the best systems for the exploration of light-induced intramolecular energy transfer. Many kinds of porphyrins and porphyrin dimers have been studied over the past decade, however little attention has been paid to the influence of paramagnetic metals on the behavior of their excited states. In this thesis, Electron Paramagnetic Resonance Spectroscopy (EPR) is used to study such compounds. After light irradiation, porphyrins easily produce a variety of excited states, which are spin polarized and can be detected by the time-resolved (TR) EPR technique. The spin polarized results for vanadyl porphyrins, their electrostatically-coupled dimers, a covalently-linked copper porphyrin-free base porphyrin dimer, and free base porphyrins are presented in this thesis. From these results we can conclude that the spin polarization patterns of vanadyl porphyrins come primarily from the trip-quartet state generated by intersystem crossing (lSC) from the excited sing-doublet state through the trip-doublet state. The spin polarization pattern of electrostatically-coupled vanadyl porphyrin-free base porphyrin dimer is produced by the triplet state of the free base porphyrin half which is coupled to the unpaired electron on the vanadyl ion.

Electron Transfer Involving the Phylloquinone (A1) Cofactor of Photosystem I Examined with Time Resolved Absorbance and Electron Paramagnetic Resonance Spectroscopy

The dependence of the electron transfer (ET) rate on the Photosystem I (PSI) cofactor phylloquinone (A1) is studied by time-resolved absorbance and electron paramagnetic resonance (EPR) spectroscopy. Two active branches (A and B) of electron transfer converge to the FX cofactor from the A1A and A1B quinone. The work described in Chapter 5 investigates the single hydrogen bond from the amino acid residue PsaA-L722 backbone nitrogen to A1A for its effect on the electron transfer rate to FX. Room temperature transient EPR measurements show an increase in the rate for the A1A- to FX for the PsaA-L722T mutant and an increased hyperfine coupling to the 2-methyl group of A1A when compared to wild type. The Arrhenius plot of the A1A- to FX ET in the PsaA-L722T mutant suggests that the increased rate is probably the result of a slight change in the electronic coupling between A1A- and FX. The reasons for the non-Arrhenius behavior are discussed. The work discussed in Chapter 6 investigates the directionality of ET at low temperature by blocking ET to the iron-sulfur clusters FX, FA and FB in the menB deletion mutant strain of Synechocyctis sp. PCC 6803, which is unable to synthesize phylloquinone, by incorporating the high midpoint potential (49 mV vs SHE) 2,3-dichloro-1,4-naphthoquinone (Cl2NQ) into the A1A and A1B binding sites. Various EPR spectroscopic techniques were implemented to differentiate between the spectral features created from A and B- branch electron transfer. The implications of this result for the directionality of electron transfer in PS I are discussed. The work discussed in Chapter 7 was done to study the dependence of the heterogeneous ET at low temperature on A1 midpoint potential. The menB PSI mutant contains plastiquinone-9 in the A1 binding site. The solution midpoint potential of the quinone measures 100 mV more positive then wild-type phylloquinone. The irreversible ET to the terminal acceptors FA and FB at low temperature is not controlled by the forward step from A1 to FX as expected due to the thermodynamic differences of the A1 cofactor in the two active branches A and B. Alternatives for the ET heterogeneity are discussed.

Time-resolved spectroscopy studies of Gd2SiO5 : Ce3+ from spherical particles

This paper reports on time-resolved emission and excitation spectra measurement studies of Gd2SiO5:Ce3+ in powder or pellet samples, from spherical particles, in order to assign the Ce3+ ion transitions into two different symmetry sites. Samples were obtained from solid-state reaction of the spherical particles oxides, SiO2 and Gd2O3:Ce3+. From time-resolved spectroscopy measurements Ce3+ ion transitions occupying the two different gadolinium crystallographic sites in Gd2SiO5 were separated and assigned. (C) 2002 Elsevier B.V. B.V. All rights reserved.

Multivariate curve resolution analysis applied to time-resolved synchrotron X-ray Absorption Spectroscopy monitoring of the activation of copper alumina catalyst

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Time-resolved random laser spectroscopy of inhomogeneously broadened systems

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Time-resolved surface enhanced resonance Raman spectro-electrochemistry of heme proteins

The membrane protein Cytochrome c Oxidase (CcO) is one of the most important functional bio-molecules. It appears in almost every eukaryotic cell and many bacteria. Although the different species differ in the number of subunits, the functional differences are merely marginal. CcO is the terminal link in the electron transfer pathway of the mitochondrial respiratory chain. Electrons transferred to the catalytic center of the enzyme conduce to the reduction of molecular oxygen to water. Oxygen reduction is coupled to the pumping of protons into the inter-membrane space and hence generates a difference in electrochemical potential of protons across the inner mitochondrial membrane. This potential difference drives the synthesis of adenosine triphosphate (ATP), which is the universal energy carrier within all biological cells. rnrnThe goal of the present work is to contribute to a better understanding of the functional mechanism of CcO by using time-resolved surface enhanced resonance Raman spectroscopy (TR-SERRS). Despite intensive research effort within the last decades, the functional mechanism of CcO is still subject to controversial discussions. It was the primary goal of this dissertation to initiate electron transfer to the redox centers CuA, heme a, heme a3 and CuB electrochemically and to observe the corresponding redox transitions in-situ with a focus on the two heme structures by using SERRS. A measuring cell was developed, which allowed combination of electrochemical excitation with Raman spectroscopy for the purpose of performing the accordant measurements. Cytochrome c was used as a benchmark system to test the new measuring cell and to prove the feasibility of appropriate Raman measurements. In contrast to CcO the heme protein cc contains only a single heme structure. Nevertheless, characteristic Raman bands of the hemes can be observed for both proteins.rnrnIn order to investigate CcO it was immobilized on top of a silver substrate and embedded into an artificial membrane. The catalytic activity of CcO and therefore the complete functional capability of the enzyme within the biomimetic membrane architecture was verified using cyclic voltammetry. Raman spectroscopy was performed using a special nano-structured silver surface, which was developed within the scope of the present work. This new substrate combined two fundamental properties. It facilitated the formation of a protein tethered bilayer lipid membrane (ptBLM) and it allowed obtaining Raman spectra with sufficient high signal-to-noise ratios.rnSpectro-electrochemical investigations showed that at open circuit potential the enzyme exists in a mixed-valence state, with heme a and and heme a3 in the reduced and oxidized state, respectively. This was considered as an intermediate state between the non-activated and the fully activated state of CcO. Time-resolved SERRS measurements revealed that a hampered electron transfer to the redox center heme a3 characterizes this intermediate state.rn