Sökning: "heme"

Visar resultat 1 - 5 av 141 avhandlingar innehållade ordet heme.

  1. 1. Porphyrins and heme in microorganisms : Porphyrin content and its relation to phototherapy and antimicrobial treatments in vivo and in vitro

    Författare :Jonas Fyrestam; Conny Östman; Jonas Bergquist; Stockholms universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Porphyrins; heme; phototherapy; antimicrobial resistance; singlet oxygen; photosensitizer; bacteria; HPLC-MS MS; oral bacteria; Aggregatibacter actinomycetemcomitans; Porphyromonas gingivalis; Escherichia coli; Analytical Chemistry; analytisk kemi;

    Sammanfattning : One of the greatest threats to human health is increasing antimicrobial resistance among pathogens, and finding alternatives for treatment of bacterial infections is of highest importance together with a more controlled use of antibiotics. Porphyrins and heme have both been shown to be a promising class of compounds for inactivation of bacteria; porphyrins by their excellent properties to act as a photosensitizer, and heme by its importance as an iron source during a bacterial infection in vertebrates. LÄS MER

  2. 2. Heme A synthase from Bacillus subtilis and Aeropyrum pernix

    Författare :Anna Lewin; Biologiska institutionen; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; heme A synthesis; heme A; heme A synthase; CtaA; cCtaA; cytochrome a; Aeropyrum pernix; Bacillus subtilis;

    Sammanfattning : Respiration in animals, plants and many bacteria is dependent on heme A, which functions as a prosthetic group in a-type cytochromes (terminal energy-transducing oxidases in the electron transport chain that reduce molecular oxygen to water). Heme A synthase catalyses a chemically very demanding reaction, the conversion of one specific methyl side-group of heme O to a formyl group of heme A. LÄS MER

  3. 3. Alpha-1-microglobulin, heme-binding protein, reductase and antioxidant

    Författare :Maria Allhorn; Infektionsmedicin; []
    Nyckelord :MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; reduction; inflammation; chronic ulcers; collagen; low density lipoproteins; Medicin människa och djur ; Medicine human and vertebrates ; antioxidation; heme; hemoglobin; alpha-1-microglobulin; lipocalin;

    Sammanfattning : This thesis describes structural and functional studies of alpha-1-microglobulin (a1m), a 26 kDa plasma and tissue protein that is evolutionarily well-conserved and belongs to the lipocalin superfamily. The lipocalins are polypeptides of 160-190-amino acids that are folded into an 8-stranded beta-barrel forming a pocket with a hydrophobic interior. LÄS MER

  4. 4. A1M: a heme and radical binding protein. A study on structure, function and mechanisms

    Författare :Sigurbjörg Rutardottir; Infektionsmedicin; []
    Nyckelord :MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; α1-microglobulin; oxidative stress; heme; radiation; reactive oxygen species; preeclampsia;

    Sammanfattning : This thesis describes functional and structural studies of the human protein α1-microglobulin (A1M), an evolutionarily well-conserved 26 kDa plasma and tissue protein mainly synthesized in the liver. A1M belongs to the lipocalin protein family. Lipocalins share a very similar structur, an 8-stranded β-barrel forming a hydrophobic pocket. LÄS MER

  5. 5. Quinone reduction sites and the role of heme in succinate:quinone reductase. Studies in Bacillus subtilis and Paracoccus denitrificans

    Författare :Mikael Matsson; Biologiska institutionen; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; carboxin; cytochrome b; electron transport; heme; quinone; Paracoccus denitrificans; Bacillus subtilis; Succinate:quinone reductase; succinate dehydrogenase; Microbiology; bacteriology; virology; mycology; Mikrobiologi; bakteriologi; virologi; mykologi;

    Sammanfattning : Succinate:quinone reductase (SQR) is an enzyme in the respiratory system of aerobic cells. SQR catalyzes two reactions, the oxidation of succinate to fumarate and the reduction of quinone to quinol. These reactions are coupled by electron transfer within the enzyme from the site of succinate oxidation to the site of quinone reduction. LÄS MER