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Inhibition of pea ferredoxin–NADP(H) reductase by Zn‐ferrocyanide
European Journal of Biochemistry, 2004Ferredoxin–NADP(H) reductases (FNRs) represent a prototype of enzymes involved in numerous metabolic pathways. We found that pea FNR ferricyanide diaphorase activity was inhibited by Zn2+ (Ki 1.57 µm). Dichlorophenolindophenol diaphorase activity was also inhibited by Zn2+ (Ki 1.80 µm), but the addition of ferrocyanide was required, indicating that the
Daniela L Catalano, Dupuy +2 more
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The NADP(H) redox couple in yeast metabolism
Antonie van Leeuwenhoek, 1986Theoretical calculations of the NADPH requirement for biomass formation indicate that in yeast this parameter is strongly dependent on the carbon and nitrogen sources used for growth. Enzyme surveys of NADPH-generating metabolic pathways and radiorespirometric studies demonstrate that in yeast the HMP pathway is the major source of NADPH.
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Archives of Biochemistry and Biophysics, 1988
An NADP/thioredoxin system, consisting of NADPH, NADP-thioredoxin reductase (NTR), and its thioredoxin, thioredoxin h, has been previously described for heterotrophic plant tissues, i.e., wheat seeds and cultured carrot cells. Until now there was no evidence for this system in green leaves.
F J, Florencio +3 more
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An NADP/thioredoxin system, consisting of NADPH, NADP-thioredoxin reductase (NTR), and its thioredoxin, thioredoxin h, has been previously described for heterotrophic plant tissues, i.e., wheat seeds and cultured carrot cells. Until now there was no evidence for this system in green leaves.
F J, Florencio +3 more
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Schistosoma mansoni ferredoxin NADP(H) oxidoreductase and its role in detoxification
Molecular and Biochemical Parasitology, 2002Ferredoxin NADP(H) oxidoreductases (FNR) are flavoenzymes that catalyze the electron transfer between NADP(H) and a wide range of compounds including ferredoxins and bacterial flavodoxins. FNRs are classified into two major groups: plant- and vertebrate-type.
Javier E, Girardini +2 more
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Eine NADP(H)-spezifische Oxidoreduktase beiCalliphora
Journal of Comparative Physiology, 1972BeiCalliphora erythrocephala Meig. wird eine NADP(H)-abhangige Oxidoreduktase nachgewiesen, die Glukose-6-phosphat und Sorbit-6-phosphat umsetzt. Das Enzym wird durch Sorbit-6-phosphat ebenso wie durch Sorbit inaktiviert. Die mit Glukose-6-phosphat erzielte maximale Aktivitat ist wenig geringer als die fur die Sorbitdehydrogenase ermittelte Grose.
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A new concept for ferredoxin–NADP(H) oxidoreductase binding to plant thylakoids
Trends in Plant Science, 2010During the evolution of photosynthesis, regulatory circuits were established that allow the precise coupling of light-driven electron transfer chains with downstream processes such as carbon fixation. The ferredoxin (Fd):ferredoxin-NADP(+) oxidoreductase (FNR) couple is an important mediator for these processes because it provides the transition from ...
J Philipp, Benz +4 more
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Crystal structure of NAD-dependent malate dehydrogenase complexed with NADP(H)
Biochemical and Biophysical Research Communications, 2005For better understanding of the coenzyme specificity in NAD-dependent MDH (tMDH) from Thermus flavus AT-62, we determined the crystal structures of tMDH-NADP(H) complex at maximally 1.65 A resolution. The overall structure is almost the same as that of the tMDH-NADH complex.
Takeo, Tomita +3 more
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NAD and NADP-dependent glutamate dehydrogenase in Hydrogenomonas H 16
Archiv f�r Mikrobiologie, 1970Hydrogenomonas H 16 synthetized two chromatographically distinct forms of glutamate dehydrogenase which differed in their thermolability. One glutamate dehydrogenase utilized NAD, the other NADP as a coenzyme.
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A computational strategy for altering an enzyme in its cofactor preference to
Coenzyme engineering, especially for altered coenzyme specificity, has been a research hotspot for more than a decade. In the present study, a novel computational strategy that enhances the hydrogen‐bond interaction between an enzyme and a coenzyme was developed and utilized to alter the coenzyme preference.
Dongbing, Cui +7 more
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On a new artificial mediator accepting NADP(H) oxidoreductase from Clostridium thermoaceticum
Journal of Biotechnology, 2000The purification and partial characterisation of an NADP(H) dependent artificial mediator accepting pyridine nucleotide oxidoreductase (AMAPOR) from the anaerobic Clostridium thermoaceticum is described. Depending on the redox potential of the artificial mediators the AMAPOR is able to regenerate NADP+ or NADPH rendering the enzyme useful for ...
H, Günther +3 more
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