Sökning: "heme proteins"

Visar resultat 21 - 25 av 56 avhandlingar innehållade orden heme proteins.

  1. 21. The complex world of proteins: Structure, function, and oligomerization of frataxin

    Författare :Christopher Söderberg; Biokemi och Strukturbiologi; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Frataxin; Friedreich s ataxia; self-assembly; protein-protein interaction; iron homeostasis; SAXS; cross-linking;

    Sammanfattning : Patients suffering from the deadly progressive neurodegenerative disease Friedreich's ataxia have reduced levels of expression of the protein frataxin. Yeast frataxin has been extensively studied in vitro, and has been shown to deliver iron to heme and iron-sulfur cluster biosynthesis, as well as to oligomerize in the presence of iron. LÄS MER

  3. 22. Microcrystallization and structural studies of proteins by serial crystallography and x-ray scattering

    Författare :Owens Uwangue; Göteborgs universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES;

    Sammanfattning : Proteins are the most complex and versatile biomolecules known, with essential roles in all cellular and physiological processes. They constitute the main structural components of cells, catalyze most biochemical reactions, regulate gene expression, modulate immune responses, and form tissues. LÄS MER

  4. 23. Structure and mechanism of iron and magnesium chelatases - at the heme-chlorophyll branch-point

    Författare :Michel Fodje; Lunds universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Molecular biophysics; pi-helix; secondary structure; AAA; porphyrin metallation; chelatase; Molekylär biofysik;

    Sammanfattning : Tetrapyrroles are synthesised through a single branched biosynthetic pathway. Heme and chlorophyll are synthesised from the common intermediate protoporphyrin IX at the heme-chlorophyll branch-point. LÄS MER

  5. 24. The Membrane-Spanning Domain of Complex I Investigated with Fusion Protein Techniques

    Författare :Maria Trane; Biokemi och Strukturbiologi; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; NuoN; NuoM; NuoL; covalent bound heme; Bacillus subtilis; Escherichia coli; membrane protein; His-tag; Cytochrome c; NADH:quinone oxidureductase; fusion protein;

    Sammanfattning : NADH:quinone oxidoreductase, or complex I, is a large, complex and poorly understood bioenergetic enzyme in the respiratory chain of living organisms. The enzyme has a conserved core structure, comprising fourteen protein subunits: Seven subunits protrude from the membrane and contain a flavin prosthetic group and eight iron-sulfur clusters that guide electrons from the oxidation of NADH towards the quinone binding site(s). LÄS MER

  7. 25. 5-Lipoxygenase : studies on the active site iron, and on the stimulatory factors Ca2+ and ATP

    Författare :Tove Hammarberg; Karolinska Institutet; Karolinska Institutet; []
    Nyckelord :non-heme iron centre; ATP binding; Ca2 binding; C2 domain;

    Sammanfattning : Human 5-lipoxygenase (5LO) is a monomeric non-heme iron enzyme, which catalyses the first two steps in the biosynthesis of leukotrienes: oxygenation of arachidonic acid to yield 5(S)-hydroperoxy-6-trans-8,11,14-cis-eicosatetraenoic acid (5-HPETE) and the subsequent dehydration to form the unstable epoxide intermediate 5(S)-trans-5,6-oxido7,9-trans-11,14-cis-eicosatetraenoic acid. The latter compound (leukotriene A4), is the precursor of the biologically active leukotrienes B4, C4, D4 and E4, which are regarded as critical mediators in asthma and other inflammatory and allergic disorders. LÄS MER