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Ferredoxin : NADP+ Oxidoreductase
2018Ferredoxin-NADP + reductase, the essential catalyst of NADP + photoreduction, is a flavoprotein ubiquitous in photosynthetic eukaryotic cells and Cyano-bacteria. The cyanobacteria enzyme has a much lower content of methionine and lysine and more histidines.
G. Zanetti, A. Allverti
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Reagentless oxidoreductase sensors
Biosensors and Bioelectronics, 1996The function of oxidoreductase biosensors is in general dependent on charge transport between the enzyme and an electrode surface by means of coenzymes or redox mediators. Reagentless biosensors should integrate these components within the very electrode area simultaneously preventing their leaking into the analyte medium and conserving their shuttle ...
Wolfgang Schuhmann, Hanns-Ludwig Schmidt
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Microbial Amine Oxidoreductases [PDF]
, 1998 The well known enzyme involved in oxidation of amines is monoamine oxidase (MAO, EC 1.1.3.4). The reason for this familiarity is the fact that this flavoprotein oxidizes amine hormones and neurotransmitters, compounds regulating the behaviour of mammalian organisms.
A. Hacisalihoglu, J. A. Duine
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THE APPEARANCE OF OXIDOREDUCTASES IN HEALING FRACTURES
Acta Pathologica Microbiologica Scandinavica Section A Pathology, 1970The activity of lactate, isocitrate, glucose‐6‐phosphate, succinate and lipoamide dehydrogenases, glutathione reductase, and cytochrome oxidase was demonstrated in the healing experimental fractures of mice. The animals were killed 1, 2, 4, 8, 10, 12 and 16 hours, and 1, 2 and 3 days after fracturing the right tibia.
J. Raekallio +2 more
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2007
Oxidoreductases constitute a very large class of enzymes. They are dehydrogenases and reductases that catalyze the removal or addition of the elements of molecular hydrogen to or from substrates. Enzymatic dehydrogenation is sometimes linked to auxiliary functions such as decarboxylation, deamination, or dehydration of the substrate, as in the actions ...
Perry A. Frey, Adrian D. Hegeman
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Oxidoreductases constitute a very large class of enzymes. They are dehydrogenases and reductases that catalyze the removal or addition of the elements of molecular hydrogen to or from substrates. Enzymatic dehydrogenation is sometimes linked to auxiliary functions such as decarboxylation, deamination, or dehydration of the substrate, as in the actions ...
Perry A. Frey, Adrian D. Hegeman
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[4] Glutathione : Dehydroascorbate oxidoreductases
1995Publisher 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 +2 more
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Plasma membrane oxidoreductases
Critical Reviews in Plant Sciences, 1989Physiological 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
2007Pyruvate 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. +3 more
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Oxidoreductases in plant plasma membranes
Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1997Electron 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 +4 more
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Protein disulphide oxidoreductases in bacteria
Trends in Biochemical Sciences, 1994Thioredoxins 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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