No description available.

In dieser Arbeit wird ein neuer Ansatz beschrieben, elektroaktive Verbindungen auf mesoporösen Elektroden zu fixieren. Dies wurde durch die Bildung eines sich selbst organisierenden Monolayers auf der Innenseite eines mesoporösen Trägers (ITO, FTO, ATO, TiO2) erreicht. Dieser Layer wurde dann vernetzt und in Richtung des Porenzentrums weiter aufgebaut durch Substitutions- Kondensations- oder Elektropolymerisations- Reaktionen. Es wurde ein Vernetzungsverfahren entwickelt, welches die Herstellung stabiler elektrochromer Bilder mit verbessertem Kontrast und einer Haltbarkeit von mehr als 18 Monaten erlaubt. Es beinhaltet die Synthesen von molekularen Einheiten mit latent vorhandenen oder voll entwickelten elektrochromen Eigenschaften. Diese Einheiten waren 4,4´- Bipyridine, die entweder mit optionalen N-Alkyl, N-Benzyl oder N-Phenyl Gruppen mit nukleophilem oder elektrophilen Eigenschaften oder mit TiO2 Ankergruppen versehen waren. Die Kaskadenreaktion ergab Elektroden mit unterschiedlichen Oberflächenkonzentrationen und unterschiedlichen Pimerisationsgraden. Darüber hinaus gelang es, die Haltbarkeit und den Kontrast so weit zu steigern, dass sie kommerziellen Ansprüchen genügen. Die Optimierung der Gegenelektroden wurde durch ein ähnliches Verfahren unter Verwendung von Ferrocen- Derivaten erreicht. Die Ladungskapazitäten, die durch Multilayer Vernetzung auf ATO-Ferrocen Elektroden erhalten wurden, waren hervorragend mit Ausnahme der Tatsache dass ein schwach grüner Farbton, verursacht durch oxidiertes Ferrocen, vorhanden war. Schließlich wurde die Kaskadenreaktion auf B12 Derivate zur Herstellung von katalytisch aktiven TiO2 Elektroden angewandt. Die mit B12 modifizierten Elektroden zeigten verbesserte Stabilität, höhere turn over - Zahlen und größere turn over -Raten im Vergleich zu unvernetzten B12 modifizierten Elektroden.

The basin-fill aquifers of the American Southwest host elevated concentrations of arsenic in groundwater due to the local geology. Limited information is available on arsenic dynamics in semi-arid and arid regions of the world. This study describes arsenic biogeochemistry and mechanisms of arsenic solubilization for a soil profile collected from the surface to the depth of groundwater in the Cache Valley Basin, Northern Utah. The first objective was to delineate mechanisms of arsenic solubilization from sediments collected at the study site. Microcosms containing site groundwater and siteoxidized and site-reduced sediments, were monitored over time to observe changes in the solubilization and oxidation state of arsenic and changes in mineral phases of arsenic and iron. The observed solubilization of arsenic was decoupled from iron reduction in the site-oxidized sediments in the presence of native organic carbon, which disagreed with the widely accepted hypothesis that arsenic solubilization is derived from microbial driven reductive dissolution of iron oxides. Carbonate minerals were defined as the mineral phase associated with arsenic that contributed to the arsenic measured in solution. The second objective was to determine how altering redox and water conditions down a profile affects arsenic geochemistry and hence solubility. Redox stratification was delineated in two sediment cores based on chemical analyses and visual observation of redox-sensitive parameters. The vadose zone released a considerable amount of arsenic, while the next zone, the carbonate enrichment zone, released the highest concentration of arsenic. Soluble arsenic was exclusively As(V) in the redox transition zone, where As was primarily associated with iron oxides. Solubilization of arsenic was limited in the deeply reduced depletion zone due to the formation of sulfide minerals. Lateral resolution of oxidation state and elemental association of arsenic at the micron scale were delineated using synchrotron-based X-ray absorption spectroscopy under Objective 3. The presence of unaltered arsenic sulfides was revealed in the vadose zone, suggesting that arsenic was inputted continuously to the ground surface. From the water table to the deeply reduced depletion zone sediments, arsenic mineral association was dominated by manganese-bearing carbonate minerals and amorphous iron oxides, which are vulnerable to groundwater fluctuation and redox-cycling.

Heme-substituted horseradish peroxidases and myoglobins were reconstituted from the apoenzyme using mesoheme and diacetyldeuteroheme. X-ray absorption spectroscopy was used to determine the dimensions of the active sites of these heme-substituted proteins, and were compared with those of the proto-hemeproteins. The change in the active-site structure corresponded with the electron withdrawing and donating effects of the different side chains. The oxidation-reduction potentials of Fe4+/Fe3+ couples of the heme-substituted proteins were measured at pH 7 with K2IrC16. The oxidation-reduction potential sequence for compound I/compound II was diacetyldeutero-> proto-> meso-in horseradish peroxidase. The oxidation-reduction potential sequence for compound II /ferric was meso-> proto-> diacetyldeutero-in both HRP and myoglobin. These results indicate that the oxidation of ferric to ferryl form may be related to a radical mechanism. A net charge theory was also proposed to explain these results.

The sarcoplasmic reticulum is an internal membrane system that controls the Ca²⁺ concentration inside muscle cells, and hence the contractile state of both skeletal and cardiac muscle. A key protein that that regulates the Ca²⁺ concentration in this membrane is known as the calcium release channel (CRC). The effects on Ca²⁺ dependent activation is of major importance in the study of CRC since other channel modifiers cannot effect the channel in the absence of Ca²⁺, or they require Ca²⁺ for maximum results. In this study of the high-affinity Ca²⁺ binding site, expected increases in total binding and shifts in the sensitivity of the channel to Ca²⁺ were observed when the pH increased or the solution redox status became more oxidative. Ranolazine, a drug used for treating Angina Pectoris (chest pain), desensitized the cardiac CRC activation but had no effect on the skeletal CRC. This selective desensitization may be the cause of Ranolazine's beneficial therapeutic effects. Both Ranolazine, and homocystein thiolactone (HCTL), a naturally occurring derivative of homocysteine, alters Ca²⁺ dependent activation by calcium without changing the number of channels found in the open state. Surprisingly the effect of HCTL was observed only in a reduced redox potential which leads to speculation that the formation of an alpha-carbon radical by HCTL on the cardiac CRC only occurs if select thiols are in a reduced state.

京都大学 / 0048 / 新制・課程博士 / 博士(工学) / 甲第19703号 / 工博第4158号 / 新制||工||1641(附属図書館) / 32739 / 京都大学大学院工学研究科航空宇宙工学専攻 / (主査)教授 吉田 英生, 准教授 岩井 裕, 教授 鈴木 基史, 教授 江口 浩一 / 学位規則第4条第1項該当 / Doctor of Philosophy (Engineering) / Kyoto University / DFAM

京都大学 / 0048 / 新制・課程博士 / 博士(工学) / 甲第20630号 / 工博第4368号 / 新制||工||1679(附属図書館) / 京都大学大学院工学研究科物質エネルギー化学専攻 / (主査)教授 安部 武志, 教授 阿部 竜, 教授 作花 哲夫 / 学位規則第4条第1項該当 / Doctor of Philosophy (Engineering) / Kyoto University / DGAM

No description available.

No description available.

CLIC1 is an intracellular membrane protein that is unusual in that it can exist in both a soluble and an integral membrane form. The manner in which this protein inserts into membranes is unknown although it is proposed to undergo a change in structure whereby it initially experiences a degree of unfolding and then refolds into its new membrane-bound conformation. This study focuses on the characterisation of CLIC1 in terms of its secondary, tertiary and quaternary structure, the determination of its conformational stability at equilibrium and the establishment of its unfolding kinetics, all under conditions of varying pH, polarity, redox conditions, temperature and ionic strength. CLIC1 was found to be most stable at pH 7.0 / 20oC. The unfolding process is two-state and cooperative, producing a DG(H2O) of ~10 kcal/mol and a m-value of ~2 kcal/mol per molar urea. A decrease in pH to 5.5 or an increase in temperature to 37oC resulted in the stabilisation of an equilibrium intermediate species under mild denaturing conditions and a destabilisation of the native state. This was further evidenced by an increase in the rate of unfolding of CLIC1 from the native state to the denatured state under these conditions. A state with similar properties to the intermediate species was detected in the absence of urea at pH 5.5 / 37oC and under non-reducing conditions at both pH 7.0 / 20oC and pH 5.5 / 20oC. The intermediate species is more hydrophobic than either the native or denatured state; it is stabilised by salts, has a reduced secondary structure, increased flexibility and a buried Trp35 relative to the native state. The rate of formation of the intermediate species is a slow process which may involve an oligomerisation step. The results from this study provide an interpretation for the structure and mechanism of CLIC1 pore formation in vivo by comparing the effects of the environment on the structure and stability of the protein.