Results 221 to 230 of about 75,190 (277)
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Thio-NADP is not an antagonist of NAADP
Cell Biochemistry and Biophysics, 1998Nicotinic acid adenine dinucleotide phosphate (NAADP) is a metabolite of NADP, which can release Ca2+ from stores that are distinct from those activated by either cyclic ADP-ribose or inositol 1,4,5-trisphosphate (IP3). It has previously been suggested that thio-NADP is a specific antagonist of NAADP (Chini et al. [1995] J. Biol. Chem. 270, 3216-3223).
Dickey, DM +3 more
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Archives of Biochemistry and Biophysics, 1965
Abstract Chlorophyllin a catalyzes the photoreduction of NADP (and NAD to a lesser extent) in the presence of ascorbate as electron donor and NADP reductase as the coupling enzyme. Photosynthetic pyridine nucleotide reductase is inactive in the reaction and does not stimulate the reaction observed with NADP reductase.
L P, VERNON, A S, PIETRO, D A, LIMBACH
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Abstract Chlorophyllin a catalyzes the photoreduction of NADP (and NAD to a lesser extent) in the presence of ascorbate as electron donor and NADP reductase as the coupling enzyme. Photosynthetic pyridine nucleotide reductase is inactive in the reaction and does not stimulate the reaction observed with NADP reductase.
L P, VERNON, A S, PIETRO, D A, LIMBACH
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Affinity labeling of spinach ferredoxin-NADP+ oxidoreductase with periodate-oxidized NADP+
Archives of Biochemistry and Biophysics, 1984Periodate-oxidized NADP+ (dialdehyde-NADP+) inactivated soluble ferredoxin-NADP+ oxidoreductase and combined covalently to the enzyme. This inactivation was first order with respect to dialdehyde-NADP+ and followed saturation kinetics, indicating that the enzyme initially forms a reversible complex with the inactivator.
R L, Chan, N, Carrillo
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Complex formation by ferredoxin-NADP+ reductase with ferredoxin or NADP+
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1973Abstract Complex formation by ferredoxin-NADP + reductase (NADPH:ferredoxin oxidoreductase, EC 1.6.99.4) with ferredoxin was measured by the independent methods based on the changes of circular dichroism, fluorescence intensity and the chromatographic behavior on a Sephadex G-75 column of the two proteins after mixing.
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Apollo-NADP+: a spectrally tunable family of genetically encoded sensors for NADP+
Nature Methods, 2016NADPH-dependent antioxidant pathways have a critical role in scavenging hydrogen peroxide (H2O2) produced by oxidative phosphorylation. Inadequate scavenging results in H2O2 accumulation and can cause disease. To measure NADPH/NADP(+) redox states, we explored genetically encoded sensors based on steady-state fluorescence anisotropy due to FRET ...
William D, Cameron +5 more
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A lysyl residue at the NADP binding site of ferredoxin-NADP reductase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1976Dansyl chloride, at low molar ratio, inactivates ferredoxin-NADP reductase (NADPH:ferredoxin oxidoreductase, EC 1.6.7.1). The complete protection afforded either by NADP or NADPH suggests a direct involvement of the active site. Experiments with [Me-14C] dansyl chloride showed that about 1.5 residues per flavin were dansylated: by differential ...
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How is ferredoxin-NADP reductase involved in the NADP photoreduction of chloroplasts?
Photosynthesis Research, 2004NADP photoreduction of chloroplasts was discovered in 1951, and subsequent research was conducted to elucidate the enzymatic mechanisms involved in this reaction. In 1963, ferredoxin-NADP reductase (FNR; EC 1.18.1.2, ferredoxin-NADP oxidoreductase) was isolated and purified to a crystalline form.
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Enzymatic Synthesis of Caged NADP Cofactors: Aqueous NADP Photorelease and Optical Properties
The Journal of Organic Chemistry, 2000The synthesis of caged NADP analogues 18, 19, and 20 has been accomplished by utilizing the transglycosidase activity of solubilized NAD glycohydrolase (porcine brain) to incorporate caged nicotinamides 2, 3, and 4 into NADP. The synthesis of several nicotinamides modified at the carboxamide with o-nitrobenzyl photolabile groups is demonstrated as well
C P, Salerno, D, Magde, A P, Patron
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Trends in Microbiology, 1998
Catabolite repression is a central multigene regulatory network that enables bacteria to select and utilize the optimal carbon and energy sources available in a given environment. Cyclic AMP and catabolite gene activator protein (CAP) play central roles in mediating catabolite repression in enteric bacteria but are absent from Gram-positive bacteria ...
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Catabolite repression is a central multigene regulatory network that enables bacteria to select and utilize the optimal carbon and energy sources available in a given environment. Cyclic AMP and catabolite gene activator protein (CAP) play central roles in mediating catabolite repression in enteric bacteria but are absent from Gram-positive bacteria ...
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Archives of Biochemistry and Biophysics, 1979
Abstract The plastidic ferredoxin-NADP + reductase from the xanthophycean alga Bumilleriopsis forms a stoichiometric 1:1 complex with ferredoxin and NADP + which is demonstrated by difference spectra of both complexes. Butanedione modification of the flavoprotein results in loss of its enzymatic activities (transhydrogenase and diaphorase ...
G, Bookjans, P, Böger
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Abstract The plastidic ferredoxin-NADP + reductase from the xanthophycean alga Bumilleriopsis forms a stoichiometric 1:1 complex with ferredoxin and NADP + which is demonstrated by difference spectra of both complexes. Butanedione modification of the flavoprotein results in loss of its enzymatic activities (transhydrogenase and diaphorase ...
G, Bookjans, P, Böger
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