The transient catalytically competent coenzyme allocation into the active site of Anabaena ferredoxin NADP+ -reductase

scientific article published on 03 May 2011

The transient catalytically competent coenzyme allocation into the active site of Anabaena ferredoxin NADP+ -reductase is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1007/S00249-011-0704-5
P698PubMed publication ID21538059

P2093author name stringJosé Ramón Peregrina
Milagros Medina
Isaías Lans
P2860cites workMechanism of the hydride transfer between Anabaena Tyr303Ser FNR(rd)/FNR(ox) and NADP+/H. A combined pre-steady-state kinetic/ensemble-averaged transition-state theory with multidimensional tunneling studyQ43159332
C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H.Q46744932
Competition between C-terminal Tyrosine and Nicotinamide Modulates Pyridine Nucleotide Affinity and Specificity in Plant Ferredoxin-NADP+ReductaseQ57971136
Molecular dynamics characterization of the active cavity of carboxypeptidase A and some of its inhibitor adductsQ68036476
Electron transfer by ferredoxin:NADP+ reductase. Rapid-reaction evidence for participation of a ternary complexQ70620888
Ferredoxin:NADP+ oxidoreductase. Equilibria in binary and ternary complexes with NADP+ and ferredoxinQ71430949
Molecular dynamics simulations of the docking of substituted N5-deazapterins to dihydrofolate reductaseQ73113098
Role of critical charged residues in reduction potential modulation of ferredoxin-NADP+ reductaseQ74236736
Catalytic mechanism of hydride transfer between NADP+/H and ferredoxin-NADP+ reductase from Anabaena PCC 7119Q79561314
Interaction of Ferredoxin-NADP(+) Reductase with its Substrates: Optimal Interaction for Efficient Electron TransferQ81358264
Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxinQ24675963
Very fast prediction and rationalization of pKa values for protein-ligand complexesQ27144110
A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studiesQ27619492
Probing the determinants of coenzyme specificity in ferredoxin-NADP+ reductase by site-directed mutagenesisQ27629226
Mechanism of coenzyme recognition and binding revealed by crystal structure analysis of ferredoxin-NADP+ reductase complexed with NADP+Q27639218
Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]Q27641437
Protein motifs involved in coenzyme interaction and enzymatic efficiency in anabaena ferredoxin-NADP+ reductaseQ27653823
Role of specific residues in coenzyme binding, charge-transfer complex formation, and catalysis in Anabaena ferredoxin NADP+-reductaseQ27661659
Involvement of Serine 96 in the Catalytic Mechanism of Ferredoxin-NADP+ Reductase: Structure-Function Relationship As Studied by Site-Directed Mutagenesis and X-ray CrystallographyQ27729902
Refined crystal structure of spinach ferredoxin reductase at 1.7 A resolution: oxidized, reduced and 2'-phospho-5'-AMP bound statesQ27730432
X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium Anabaena PCC 7119 at 1.8 A resolution, and crystallographic studies of NADP+ binding at 2.25 A resolutionQ27733738
Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductaseQ27766345
VMD: visual molecular dynamicsQ27860554
SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelingQ27860614
The Amber biomolecular simulation programsQ27860745
Conformational Changes Combined with Charge-Transfer Interactions Are Essential for Reduction in Catalysis by p-Hydroxybenzoate HydroxylaseQ30335777
Modulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site.Q30367807
Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxinQ31061888
Involvement of glutamic acid 301 in the catalytic mechanism of ferredoxin-NADP+ reductase from Anabaena PCC 7119.Q32107354
Mechanistic insights into ferredoxin-NADP(H) reductase catalysis involving the conserved glutamate in the active siteQ34096947
Open questions in ferredoxin‐NADP+ reductase catalytic mechanismQ34192164
Induced fit and equilibrium dynamics for high catalytic efficiency in ferredoxin-NADP(H) reductasesQ34980565
Structural and mechanistic aspects of flavoproteins: photosynthetic electron transfer from photosystem I to NADP+.Q34991037
Electron transfer by diflavin reductases.Q35737692
Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases.Q35768735
The role of cysteine residues of spinach ferredoxin-NADP+ reductase As assessed by site-directed mutagenesis.Q38318119
Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxinQ42080846
A redox-dependent interaction between two electron-transfer partners involved in photosynthesisQ42111452
Binding thermodynamics of ferredoxin:NADP+ reductase: two different protein substrates and one energeticsQ42151421
Exact analysis of heterotropic interactions in proteins: Characterization of cooperative ligand binding by isothermal titration calorimetryQ42720831
P433issue1
P304page(s)117-128
P577publication date2011-05-03
P1433published inEuropean Biophysics JournalQ5412316
P1476titleThe transient catalytically competent coenzyme allocation into the active site of Anabaena ferredoxin NADP+ -reductase
P478volume41

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cites work (P2860)
Q87055499A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme
Q27679819Crystal Structure of the FAD-Containing Ferredoxin-NADP+Reductase from the Plant PathogenXanthomonas axonopodispv. citri
Q38637109High-resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily
Q39210413Interaction and electron transfer between ferredoxin-NADP(+) oxidoreductase and its partners: structural, functional, and physiological implications.

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