Sökning: "NADH dehydrogenases"
Visar resultat 6 - 10 av 14 avhandlingar innehållade orden NADH dehydrogenases.
6. Gene description, activity quantification and physiological responses of mitochondrial alternative NAD(P)H dehydrogenases
Sammanfattning : In addition to proton-pumping complex I, the plant respiratory chain contains type II NAD(P)H dehydrogenases. These extra enzymes do not pump protons and consequently do not contribute to the electrochemical proton gradient. LÄS MER
7. Identification and characterization of novel mammalian alcohol dehydrogenases
Sammanfattning : The vertebrate medium chain alcohol dehydrogenases are dimeric zinc metalloenzymes that catalyze the reversible oxidation/reduction of alcohols/aldehydes using NAD+/NADH as coenzyme. In mammals, six classes of ADH have been defined (ADH1-ADH6) whereof five have been identified in humans. LÄS MER
8. The plant respiratory chain: Redox responses and catalytic definition of alternative pathways
Sammanfattning : The respiratory chain of plants contains both proton-pumping enzymes that conserve energy and non-proton-pumping alternative enzymes that bypass the sites of energy conservation. In addition to the proton-pumping complex I, plant mitochondria contain alternative type II NAD(P)H dehydrogenases, which allow oxidation of NADH and NADPH from the matrix and the cytosol. LÄS MER
9. Characterization of stress-inducible short-chain dehydrogenases/reductases (SDR) in plants : study of a novel small protein family from Pisum sativum (pea)
Sammanfattning : In pea (Pisum sativum), the short-chain alcohol dehydrogenase-like protein (SAD) gene family consists of at least three members (SAD-A, -B, and -C). The SAD genes are transiently expressed in plants after short exposures to ultraviolet-B radiation, which in turn leads to formation of SAD protein in leaf and stem tissue upon prolonged irradiation. LÄS MER
10. Alternative NAD(P)H dehydrogenases in plant mitochondria - localisation, catalytic functions and physiological roles
Sammanfattning : In addition to complex I, the plant mitochondrial electron transport chain possesses several alternative NAD(P)H dehydrogenases, not present in animals. These enzymes allow nonenergy-conserving electron transfer from cytoplasmic and matrix NAD(P)H to ubiquinone. LÄS MER