Search for dissertations about: "thiol-disulfide oxidoreductases"

Showing result 1 - 5 of 7 swedish dissertations containing the words thiol-disulfide oxidoreductases.

  1. 1. Membrane-bound thiol-disulfide oxidoreductases in Bacillus subtilis

    Author : Lydur Erlendsson; Institutionen för experimentell medicinsk vetenskap; []
    Keywords : MEDICIN OCH HÄLSOVETENSKAP; MEDICAL AND HEALTH SCIENCES; virologi; mykologi; Mikrobiologi; mycology; virology; bacteriology; Microbiology; sporulation; cytochrome c; thiol-disulfide oxidoreductases; Bacillus subtilis; membrane proteins; bakteriologi;

    Abstract : Disulfide bonds in proteins are found between cysteine residues and are usually important for either function or stability of proteins. Thiol-disulfide oxidoreductases catalyse the formation or breakage of disulfide bonds in proteins. READ MORE

  2. 2. Studies on Thiol-Disulfide Oxidoreductases in Bacillus subtilis

    Author : Mirja Carlsson Möller; Molekylär cellbiologi; []
    Keywords : NATURVETENSKAP; NATURAL SCIENCES; virology; mycology; Mikrobiologi; bakteriologi; virologi; mykologi; Microbiology; bacteriology; bacterial sporulation; endospore; thioredoxin; Thiol-disulfide oxidoreductase;

    Abstract : Bacillus subtilis is a model organism for endospore-forming gram-positive bacteria. Endospores are formed in response to nutrient starvation. They can resist harsh environments and last for long periods of time. Once nutrients again become available, the endospore can germinate and the vegetative life cycle be resumed. READ MORE

  3. 3. Structure-function studies of glutaredoxins and related oxidoreductases

    Author : Tobias Elgán; Karolinska Institutet; Karolinska Institutet; []
    Keywords : Thiol-disulfide oxidoreductase; thioredoxin; Trx; glutaredoxin; Grx; protein disulfide oxidoreductase; PDO; -C-X-X-C-; specificity; conformational stability; ligandinduced stability; CD spectroscopy; redox potential;

    Abstract : The members of the ubiquitous group of thiol-disulfide oxidoreductases are characterized by a conserved tertiary structure, the thioredoxin (Trx) fold, and by having a consensus -C-X-X-C- active site sequence motif. By utilizing the active site cysteines, these proteins participate in redox reactions by catalyzing reversible disulfide oxidation and reduction. READ MORE

  4. 4. Biochemical properties of human glutaredoxins

    Author : Catrine Johansson; Karolinska Institutet; Karolinska Institutet; []
    Keywords : ;

    Abstract : Glutaredoxins (Grxs) are highly conserved thiol-disulfide oxidoreductases that utilize electrons from the tripeptide glutathione (GSH) to catalyze thiol-disulfide exchange reactions. Bacteria, yeast and plants contain multiple dithiol Grxs, which are involved in different cellular processes like DNA synthesis, defense against oxidative stress, apoptosis, and regulation of transcription factor binding activity. READ MORE

  5. 5. In vivo functions of mammalian glutaredoxin 2

    Author : Maria Lönn; Karolinska Institutet; Karolinska Institutet; []
    Keywords : ;

    Abstract : Oxygen is essential for all respirating life forms. However, the use of molecular oxygen as terminal electron acceptor of the respiratory electron chain leads to the generation of reactive oxygen species (ROS) as product of incomplete oxygen reduction. To different extends, ROS can react with and damage DNA, lipids and proteins. READ MORE