Sökning: "Fe – S clusters"
Visar resultat 1 - 5 av 11 avhandlingar innehållade orden Fe – S clusters.
1. Frameshifting as a tool in analysis of transfer RNA modification and translation
Sammanfattning : Studies of ribosomal reading frame maintenance are often based on frameshift mutation suppression experiments. In this thesis, suppression of a frameshift mutation in Salmonella enterica serovar Typhimurium by a tRNA and a ribosomal protein are described. LÄS MER
2. Iron Carbonyl Clusters as Proton Reduction Catalysts
Sammanfattning : Abstract – The mixed-valence triiron complexes [Fe3(CO)7-x(PPh3)x(µ-edt)2] (x = 0, 1, 2; edt = SCH2CH2S) and [Fe3(CO)5(κ2-diphosphine)(µ-edt)2] (diphosphine = dppv, dppe, dppb, dppn) have been prepared and structurally characterized. In comparison to the diiron complex [Fe2(CO)6(µ-edt)], [Fe3(CO)7(µ-edt)2] catalyzes proton reduction at 0. LÄS MER
3. Viperin, a multifunctional radical SAM enzyme : biogenesis and antiviral mechanisms
Sammanfattning : Viperin (virus-inhibitory protein, endoplasmic reticulum-associated, interferon-inducible) is an interferon-induced antiviral protein. It has three distinct functional domains: the N-terminal domain, the radical SAM (S-adenosylmethionine) domain for binding iron-sulphur cluster, and the C-terminus domain. LÄS MER
4. Formation of Thiolated Nucleosides in tRNA in Salmonella enterica serovar typhimurium
Sammanfattning : The presence and synthesis of transfer RNA (tRNA) is highly conserved in all organisms and a lot of genetic material is dedicated to its synthesis. tRNA contains a large number of modified nucleosides and several diverse functions have been found but much about their function is still unknown. LÄS MER
5. Theoretical studies of porphyrin proteins
Sammanfattning : Different aspects of porphyrin proteins have been studied with theoretical methods. For example, we have studied: - The importance of hydrogen bonds for the discrimination between carbon monoxide and molecular oxygen by myoglobin, the oxygen carrier in muscles, modelling the active site both in vacuum and in the protein matrix - The inner-sphere reorganisation energy during electron transfer for cytochromes compared to other electron-transfer proteins, such as blue copper proteins and Fe-S clusters - The role of porphyrin distortions in the reaction mechanism of ferrochelatase, the enzyme that inserts an iron ion into protoporphyrin IX to make haem - The interaction between different metal sites in ferrochelatase In these studies we have used density functional theory, classical force field methods, and a combination of quantum chemistry and molecular mechanics. LÄS MER