Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin.
about
The long goodbye: the rise and fall of flavodoxin during plant evolutionModulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site.Structural and mechanistic aspects of flavoproteins: electron transfer through the nitric oxide synthase flavoprotein domain.Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance.A mobile tryptophan is the intrinsic charge transfer donor in a flavoenzyme essential for nikkomycin antibiotic biosynthesis.Ectopic expression of a cyanobacterial flavodoxin in creeping bentgrass impacts plant development and confers broad abiotic stress tolerance.Engineering the future. Development of transgenic plants with enhanced tolerance to adverse environments.The importance of flavodoxin for environmental stress tolerance in photosynthetic microorganisms and transgenic plants. Mechanism, evolution and biotechnological potential.High-resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily.Interaction and electron transfer between ferredoxin-NADP(+) oxidoreductase and its partners: structural, functional, and physiological implications.Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP(+) oxidoreductase activity toward NADPH.Engineering of versatile redox partner fusions that support monooxygenase activity of functionally diverse cytochrome P450s.Design and improvement of artificial redox modules by molecular fusion of flavodoxin and flavodoxin reductase from Escherichia coliDocking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin.Binding thermodynamics of ferredoxin:NADP+ reductase: two different protein substrates and one energeticsExact analysis of heterotropic interactions in proteins: Characterization of cooperative ligand binding by isothermal titration calorimetry.C-terminal tail residue Arg1400 enables NADPH to regulate electron transfer in neuronal nitric-oxide synthase.C-terminal residues of ferredoxin-NAD(P)(+) reductase from Chlorobaculum tepidum are responsible for reaction dynamics in the hydride transfer and redox equilibria with NADP(+)/NADPH.Flavodoxin displays dose-dependent effects on photosynthesis and stress tolerance when expressed in transgenic tobacco plants.Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase.
P2860
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P2860
Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Role of the C-terminal tyrosin ...... ers ferredoxin and flavodoxin.
@ast
Role of the C-terminal tyrosin ...... ers ferredoxin and flavodoxin.
@en
type
label
Role of the C-terminal tyrosin ...... ers ferredoxin and flavodoxin.
@ast
Role of the C-terminal tyrosin ...... ers ferredoxin and flavodoxin.
@en
prefLabel
Role of the C-terminal tyrosin ...... ers ferredoxin and flavodoxin.
@ast
Role of the C-terminal tyrosin ...... ers ferredoxin and flavodoxin.
@en
P2093
P356
P1433
P1476
Role of the C-terminal tyrosin ...... ers ferredoxin and flavodoxin.
@en
P2093
Carlos Gómez-Moreno
Darío Paladini
Eduardo A Ceccarelli
Gordon Tollin
Isabel Nogués
Jesús Tejero
John K Hurley
Milagros Medina
Néstor Carrillo
Stephen G Mayhew
P304
P356
10.1021/BI049858H
P407
P577
2004-05-01T00:00:00Z