Browsing by Subject "Mossbauer spectroscopy"
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Item Atomic and nuclear interference phenomena and their applications(Texas A&M University, 2005-08-29) Kuznetsova, Yelena AnatolyevnaIn this work, interference and coherence phenomena, appearing in atomic and molecular ensembles interacting with coherent light sources, as electromagnetically induced transparency (EIT), coherent population trapping (CPT), and slow group velocity of light are investigated. The goal of the project is to make the steps towards various applications of these phenomena, first, by studying them in solid media (which are the most advantageous for applications), second, by suggesting some novel applications such as CPT-based plasma diagnostics, and realization of new types of solid-state lasers (based on suppression of excited-state absorption via EIT). The third goal of the project is extension of coherence and interference effects well-known in optics to the gamma-ray range of frequencies and, correspondingly, from atomic to nuclear transitions. A particular technique of chirped pulse compression applied to M??ossbauer transitions is considered and the possibility of compression of M??ossbauer radiation into ultrashort gamma-ray pulses is analyzed. The theoretical treatment of the interference and coherence effects is based on the semiclassical description of atom-light interaction, which is sufficient for correct analysis of the phenomena considered here. Coherent media are considered in two-, three-, and four-level approximations while their interaction with light is studied both analytically and numerically using the Maxwell-Bloch set of equations.Item Bioinspired Synthesis and Reactivity Studies of Nitric Oxide Iron Complexes(2012-02-14) Hess, JenniferThe significant role that nitric oxide plays in human physiology is linked to the ability of NO to bind to iron forming mono-nitrosyl iron complexes. Protein-bound and low-molecular-weight dinitrosyl iron complexes (DNICs) are known to form in excess NO. Studies of such biological DNICs have relied on their paramagnetism and characteristic EPR signal of g value of 2.03. It has been suggested that DNICs act in vivo as NO storage (when protein-bound) and transfer agents (when released by, for example, free cysteine). Biological DNICs, mainly resulting from iron-sulfur cluster degradation, are difficult to extract and isolate, thereby preventing their full characterization. Thus, development of synthetic DNICs is a promising approach to model and better understand the formation and function of biological DNICs, the scope of donor ligands that might coexist with Fe(NO)2 units, the redox levels of bio-DNICs, and establish other spectroscopic techniques appropriate for characterization. A series of N-heterocyclic carbene (NHC) and imidazole (Imid) complexes has been characterized as mimics of histidine-containing DNICs. The pseudo-tetrahedral L2Fe(NO)2 complexes have NO stretching frequencies and redox potentials that suggest the NHCs are slightly better donors than Imids, however the two types of ligands have similar steric properties. Both the EPR-active, {Fe(NO)2}9 and the EPR-silent, {Fe(NO)2}10 states can be accessed and stabilized by the NHC. Nitric oxide transfer studies have shown that only the {Fe(NO)2}9 complexes are capable of transferring NO to a suitable NO trapping agent. Deprotonation of the distal nitrogen functionality in the imidazolate ligands of [(Imidazole)2Fe(NO)2]- leads to aggregation forming molecular squares of {Fe(NO)2}9 units bridged by the imidazolates. These interesting tetrameric complexes are examined by X-ray diffraction, EPR, and M?ssbauer studies. The paramagnetic tetrameric complexes have multiple redox events observed by cyclic voltammetry. M?ssbauer spectral data of the tetrameric complexes are compared with M?ssbauer data obtained for a series of NHC-containing DNICs. Iron and cobalt-containing mononitrosyl N2S2 model complexes of the nitrile hydratase enzyme active site demonstrate sulfur-based reactivity resulting in the formation of polymetallic complexes. In all cases, shifts in the nitrosyl stretching frequencies demonstrate substantial transfer of electron density from the (NO)M(N2S2) moiety to the metal-acceptor site.Item Probing Iron Accumulation in Sacchromyces cerevisiae Using Integrative Biophysical and Biochemical Techniques(2012-02-14) Miao, RenIron is an essential element for life. It is involved in a number of biological processes, including iron sulfur (Fe/S) cluster assembly and heme biosynthesis. However it is also potentially toxic due to its ability to induce formation of reactive oxygen species (ROS) via Fenton chemistry. Therefore its uptake, trafficking and utilization must be regulated to avoid its toxicological effect. It has been recently discovered that Fe/S cluster biosynthesis machinery plays a key role in the cellular iron regulation and its disruption leads to impaired iron regulation and iron accumulation within mitochondria. The iron accumulation resulted from impaired Fe/S cluster assembly in the eukaryotic model organism Saccharomyces cerevisiae (baker?s yeast) was studied. Various biophysical (e.g. M?ssbauer, EPR, UV-vis spectroscopy) and biochemical (e.g. Western blots, PCR, enzyme activity assay, etc.) techniques were used to characterize the iron content in yeast mitochondria isolated from several mutants strains. In these mutants one of the proteins involved in Fe/S cluster biosynthesis (Yah1p and Atm1p) is mutated and iron regulation and metabolism are disrupted. By integrating the results obtained from these different methods, it was determined that excess iron accumulates in the mutant mitochondria as inorganic phosphate Fe(III) nano-particles exhibiting superparamagnetic behaviors. Oxygen is required for iron accumulation and nanoparticle formation. The Fe(III) nano-particles can be chemically reduced to Fe(II) then largely exported from the mitochondria. These biophysical and biochemical methods were also used to examine the iron distribution in whole yeast cells of the Aft1-1up strain in which iron regulon genes are constitutively activated and compared to that of Yah1p-depleted and wild type yeast. Constitutive activation of iron regulon genes does not alter the cellular iron distribution significantly. However disruption of Fe/S cluster assembly by Yah1p depletion causes dramatic cellular iron redistribution: the vacuolar iron is largely evacuated and most of the cellular iron probably precipitates in mitochondria as Fe(III) nanoparticles. The results provide novel insights into iron trafficking and possible signal communications between organelles within cells.Item Spectroscopic and analytical characterization of the distribution of iron in intact mitochondria from Saccharomyces cerevisiae(Texas A&M University, 2006-10-30) Hudder, Brandon NealElectron paramagnetic resonance (EPR) and M????ssbauer spectroscopy were used to examine the distribution of iron in mitochondria from Saccharomyces cerevisiae. These organelles were packed into EPR and M????ssbauer cuvettes, affording spectra with unprecedented signal/noise ratios. EPR spectra of as-isolated intact mitochondria exhibited fourteen distinct signals, some of which were assigned according to previously reported g-values obtained using isolated proteins. Signals from adventitious manganese (II) and iron (III) were largely removed when mitochondria were isolated in buffers supplemented with the metal chelators EDTA or EGTA. Signals were simulated and intensities were quantified to afford spin concentrations and estimates of the concentration of EPR-active species in mitochondria. The effects of treating samples with chemical modifiers were examined. Packed samples were analyzed for protein and metal content, affording averaged values of 50 mg/mL [protein], 590 ????M [Fe], 340 ????M [Cu], and 17 ????M [Mn]. 57Fe-enriched intact mitochondria isolated in the presence of metal chelators exhibited M????ssbauer spectra dominated by three components. Approximately 60% of the 57Fe in the sample gave rise to a quadrupole doublet, most of which was diamagnetic. The parameters of this doublet are typical of S = 0 [4Fe-4S]2+ clusters and S = 0 ferrous heme groups. Spectra of samples reduced with dithionite, pH 8.5, suggested that at least half of this doublet arose from [4Fe-4S]2+ clusters. The second major component exhibited in the M????ssbauer spectra arose from high-spin ferrous ions (10%-30%). The third major component (15%) came from iron exhibiting magnetic hyperfine interactions and is likely reflected in the Fe-containing species observed by EPR. The results presented here suggest that mitochondria contain ~ 600 ????M of Fe overall, ~ 200 ?????? 400 ????M organized as [4Fe-4S]2+ clusters, with about 25 ????M due to the [4Fe-4S]2+ cluster of aconitase. Approximately 60 ????M ?????? 200 ????M of the Fe in mitochondria is high-spin ferrous ions, ~ 40 ????M as the Rieske S = 1/2 [2Fe-2S]+ cluster of cytochrome bc1, and ~20 ????M as the S = 1/2 [2Fe-2S]+ cluster of succinate dehydrogenase. The high-spin ferric hemes of the a3:CuB site of cytochrome oxidase and cytochrome c peroxidase each account for ~ 4 ????M of Fe.