Results 271 to 280 of about 43,837 (307)

[4] Glutathione : Dehydroascorbate oxidoreductases

1995
Publisher Summary This chapter focuses on the dehydroascorbate oxidoreductases of glutathione. Dehydro- L -ascorbic acid (DHA), the first chemically stable oxidation product of L -ascorbic acid (AAH 2 ), is generated in plant or animal cells from L -ascorbic acid by one- or two-electron oxidation reactions in which semidehydroascorbic acid (AAH . )
Michael P. Washburn, William W. Wells, Dian Peng Xu   +2 more
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Plasma membrane oxidoreductases

Critical Reviews in Plant Sciences, 1989
Physiological roles have been proposed for several of these enzymes which include a hormone controlled transmembrane WADH oxidase, an iron chelate reductase, nitrate reductase, cyt b 5 reductase and peroxidase. The auxin stimulated oxidase has been proposed to be involved in control of cell elongation or proliferation and the iron chelate reductase in
Frederick L. Crane, Rita Barr
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Pyruvate-Ferredoxin Oxidoreductase

2007
Pyruvate decarboxylation in many anaerobic organisms is catalyzed by the thiamine diphosphate (ThDP)-dependent pyruvate–ferredoxin oxidoreductase. We have determined the native structure of this ancient enzyme, as well as of several reaction intermediates, by soaking crystals in a pyruvate-containing solution.
Chabriere, E., Cavazza, C., Contreras-Martel, Carlos, Fontecilla-Camps, J.C.   +3 more
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Oxidoreductases in plant plasma membranes

Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1997
Electron transporting oxidoreductases at biological membranes mediate several physiological processes. While such activities are well known and widely accepted as physiologically significant for other biological membranes, oxidoreductase activities found at the plasma membrane of plants are still being neglected.
Sabine Lüthje, Sigrid Heuer, Hartwig Lüthen, Olaf Döring, Michael Böttger   +4 more
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Protein disulphide oxidoreductases in bacteria

Trends in Biochemical Sciences, 1994
Thioredoxins and eukaryotic protein disulphide isomerases were, until recently, the only enzymes known to catalyse reversible oxidation and reduction of cysteine residues of a wide spectrum of protein substrates. Genetic and biochemical investigations on different bacterial systems have now led to the discovery of novel prokaryotic protein disulphide ...
Hannes Loferer, Hauke Hennecke
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Pentitol oxidoreductases inSclerotinia sclerotiorum

Archiv f�r Mikrobiologie, 1973
Pentitol: NADP and pentitol: NAD oxidoreductase were detected in cell-free extracts of mycelia and sclerotia ofSclerotinia sclerotiorum (Lib.) D By. grown on synthetic liquid medium containingd-xtlose,l-arabinose ord-ribose. Both enzymes were similar to those reported from other fungi. The enzymes were not detected when the fungus was grown on a medium
Sy-Ying C. Wang, Duane Le Tourneau
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Oxidoreductases and Oxygenases

1984
Oxidoreductases (dehydrogenases or oxidases) catalyze the addition or the removal of hydrogen or electrons. Oxygenases bring about the incorporation of oxygen which originates from molecular oxygen.
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Bacterial NADH-quinone oxidoreductases

Journal of Bioenergetics and Biomembranes, 1991
The NADH-quinone oxidoreductases of the bacterial respiratory chain could be divided in two groups depending on whether they bear an energy-coupling site. Those enzymes that bear the coupling site are designated as NADH dehydrogenase 1 (NDH-1) and those that do not as NADH dehydrogenase 2 (NDH-2).
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Physiological Roles of Xanthine Oxidoreductase

Drug Metabolism Reviews, 2004
Xanthine oxidoreductase (XOR) is a major protein component of the milk fat globule membrane (MFGM) surrounding fat droplets in milk and its enzymology is well characterised. The enzyme is widely distributed in mammalian tissues and is generally accepted to be a key enzyme of purine catabolism.
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Glycolate oxidoreductase in Escherichia coli

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
Abstract Escherichia coli cells growing on glycolate as a sole source of carbon synthesise an enzyme which catalyses the oxidation of this compound to glyoxylate. The formation of glyoxylate from glycolate by extracts of such cells is dependent upon the presence of the artificial electron acceptors phenazine methosulphate and 2,6 ...
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