Sökning: "Martin Högbom"
Visar resultat 1 - 5 av 7 avhandlingar innehållade orden Martin Högbom.
Sammanfattning : Diiron carboxylate proteins contain a cofactor that consists of two iron atoms coordinated by carboxylate and histidine ligands. These proteins perform a multitude of chemical reactions in the cell that generally involve activation of molecular oxygen at the diiron site. LÄS MER
2. Structural studies of R2 and R2–like proteins with a heterodinuclear Mn/Fe cofactor and enzymes involved in Mycobacterium tuberculosis lipid metabolism
Sammanfattning : Tuberculosis is a notorious disease responsible for the deaths of 1.4 million people worldwide. A third of the world's population is infected with Mycobacterium tuberculosis, the bacterium causing the disease. LÄS MER
3. Structural basis for metalloprotein catalysis : Characterization of Mycobacterium tuberculosis phosphatidylinositol phosphate synthase PgsA1 and Bacillus anthracis ribonucleotide reductase R2
Sammanfattning : About a third of all proteins need to associate with a particular metal ion or metallo-inorganic cofactor to function. This interplay expands the catalytic repertoire of enzymes and reflects the adaption of these catalytic macromolecules to the environments they have evolved in. LÄS MER
4. Structural elements involved in protein-mediated proton transfer : Implications from studies of cytochrome c oxidase
Sammanfattning : Proton transfer is one of the most common reactions in biological systems. During energy conversion inside a cell, proton transfer is crucial to maintain an electrochemical proton gradient across the cell membrane. This gradient is in turn used to e.g. LÄS MER
5. Structural and Functional Studies of Membrane Proteins : From Characterisation of a Fatty Acyl-CoA Synthetase to the Discovery of Superoxide Oxidase
Sammanfattning : This thesis is divided into three parts; the first part describes a method for efficient screening of membrane proteins for crystallography. By utilising the properties of a folding reporter GFP it is possible to quickly and accurately screen the stability of a protein in a range of conditions without full purification. LÄS MER