scholarly article | Q13442814 |
P50 | author | Juan Fernández-Recio | Q40704521 |
Ruben Abagyan | Q44682954 | ||
P2093 | author name string | Milagros Medina | |
Carlos Gómez-Moreno | |||
P2860 | cites work | Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes | Q24654975 |
A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by protein engineering and crystallographic studies | Q27619492 | ||
Refined X-ray structures of the oxidized, at 1.3 A, and reduced, at 1.17 A, [2Fe-2S] ferredoxin from the cyanobacterium Anabaena PCC7119 show redox-linked conformational changes | Q27620923 | ||
Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module | Q27624980 | ||
Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis | Q27627708 | ||
Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase | Q27629524 | ||
Role of a cluster of hydrophobic residues near the FAD cofactor in Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal complex formation and electron transfer to ferredoxin | Q27631672 | ||
Probing the role of glutamic acid 139 of Anabaena ferredoxin-NADP+ reductase in the interaction with substrates | Q27639835 | ||
Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S] | Q27641437 | ||
Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at 2 A resolution | Q27642035 | ||
Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa | Q27646770 | ||
Tuning of the FMN binding and oxido-reduction properties by neighboring side chains in Anabaena flavodoxin | Q27648666 | ||
Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120 | Q27652971 | ||
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 resolution | Q27733738 | ||
Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants | Q27742765 | ||
Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP+ reductase for optimal NADP+ binding and electron transfer | Q27766746 | ||
Structure of the Escherichia coli fumarate reductase respiratory complex | Q28137751 | ||
Assessment of CAPRI predictions in rounds 3-5 shows progress in docking procedures | Q28258469 | ||
Protein interactions in the human methionine synthase-methionine synthase reductase complex and implications for the mechanism of enzyme reactivation | Q28300412 | ||
Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family | Q30195728 | ||
Prediction of protein-protein interactions by docking methods. | Q30329611 | ||
Flavin photochemistry in the analysis of electron transfer reactions: role of charged and hydrophobic residues at the carboxyl terminus of ferredoxin-NADP(+) reductase in the interaction with its substrates | Q31055470 | ||
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 | Q31061888 | ||
Role of hydrophobic interactions in the flavodoxin mediated electron transfer from photosystem I to ferredoxin-NADP+ reductase in Anabaena PCC 7119. | Q31131960 | ||
Involvement of glutamic acid 301 in the catalytic mechanism of ferredoxin-NADP+ reductase from Anabaena PCC 7119. | Q32107354 | ||
Open questions in ferredoxin‐NADP+ reductase catalytic mechanism | Q34192164 | ||
Visualization of transient encounter complexes in protein-protein association. | Q34575140 | ||
Structure-function relationships in Anabaena ferredoxin/ferredoxin:NADP(+) reductase electron transfer: insights from site-directed mutagenesis, transient absorption spectroscopy and X-ray crystallography | Q34659488 | ||
Soft protein-protein docking in internal coordinates | Q36639007 | ||
Further characterization by site-directed mutagenesis of the protein-protein interface in the ferredoxin/ferredoxin:NADP+ reductase system from Anabaena: requirement of a negative charge at position 94 in ferredoxin for rapid electron transfer | Q36734854 | ||
Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash photolysis | Q36768979 | ||
Definition of the interaction domain for cytochrome c on cytochrome c oxidase. III. Prediction of the docked complex by a complete, systematic search | Q41710393 | ||
A redox-dependent interaction between two electron-transfer partners involved in photosynthesis | Q42111452 | ||
Anabaena sp. PCC 7119 flavodoxin as electron carrier from photosystem I to ferredoxin-NADP+ reductase. Role of Trp(57) and Tyr(94). | Q43957778 | ||
Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase. | Q44945441 | ||
Anabaena flavodoxin as an electron carrier from photosystem I to ferredoxin-NADP+ reductase. Role of flavodoxin residues in protein-protein interaction and electron transfer. | Q45209006 | ||
Improving CAPRI predictions: optimized desolvation for rigid-body docking | Q46568966 | ||
ICM-DISCO docking by global energy optimization with fully flexible side-chains | Q46664729 | ||
Flavodoxin-mediated electron transfer from photosystem I to ferredoxin-NADP+ reductase in Anabaena: role of flavodoxin hydrophobic residues in protein-protein interactions | Q46821908 | ||
An electrochemical, kinetic, and spectroscopic characterization of [2Fe-2S] vegetative and heterocyst ferredoxins from Anabaena 7120 with mutations in the cluster binding loop | Q47800362 | ||
Efficient restraints for protein-protein docking by comparison of observed amino acid substitution patterns with those predicted from local environment | Q48548372 | ||
Identification of protein-protein interaction sites from docking energy landscapes. | Q52005983 | ||
Involvement of lysine-88 of spinach ferredoxin-NADP+ reductase in the interaction with ferredoxin. | Q54633642 | ||
Cell biology: brief encounters bolster contacts. | Q55042605 | ||
Structural analysis of interactions for complex formation between Ferredoxin-NADP+ reductase and its protein partners | Q60633209 | ||
Charge reversal mutations in a conserved acidic patch in Anabaena ferredoxin can attenuate or enhance electron transfer to ferredoxin:NADP+ reductase by altering protein/protein orientation within the intermediate complex | Q71530860 | ||
Ferredoxin-NADP(+) reductase uses the same site for the interaction with ferredoxin and flavodoxin | Q73154558 | ||
Highly nonproductive complexes with Anabaena ferredoxin at low ionic strength are induced by nonconservative amino acid substitutions at Glu139 in Anabaena ferredoxin:NADP+ reductase | Q73185525 | ||
Transient protein interactions studied by NMR spectroscopy: the case of cytochrome C and adrenodoxin | Q73499928 | ||
Lys75 of Anabaena ferredoxin-NADP+ reductase is a critical residue for binding ferredoxin and flavodoxin during electron transfer | Q77349788 | ||
Role of neighboring FMN side chains in the modulation of flavin reduction potentials and in the energetics of the FMN:apoprotein interaction in Anabaena flavodoxin | Q81070268 | ||
Interaction of Ferredoxin-NADP(+) Reductase with its Substrates: Optimal Interaction for Efficient Electron Transfer | Q81358264 | ||
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 848-862 | |
P577 | publication date | 2008-08-01 | |
P1433 | published in | Proteins | Q7251514 |
P1476 | title | Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin | |
P478 | volume | 72 |
Q48048896 | A physical picture for mechanical dissociation of biological complexes: from forces to free energies. |
Q42151421 | Binding thermodynamics of ferredoxin:NADP+ reductase: two different protein substrates and one energetics |
Q41642027 | Combined computational and experimental analysis of a complex of ribonuclease III and the regulatory macrodomain protein, YmdB |
Q39210413 | Interaction and electron transfer between ferredoxin-NADP(+) oxidoreductase and its partners: structural, functional, and physiological implications. |
Q50948523 | Mechanostability of the Single-Electron-Transfer Complexes of Anabaena Ferredoxin-NADP(+) Reductase. |
Q35730258 | Pseudomonas aeruginosa IscR-Regulated Ferredoxin NADP(+) Reductase Gene (fprB) Functions in Iron-Sulfur Cluster Biogenesis and Multiple Stress Response. |
Q34094541 | Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase |
Q84020930 | The transient catalytically competent coenzyme allocation into the active site of Anabaena ferredoxin NADP+ -reductase |
Q45096401 | Why is F19Ap53 unable to bind MDM2? Simulations suggest crack propagation modulates binding. |
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