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
about
The evolution, metabolism and functions of the apicoplastUnusual folded conformation of nicotinamide adenine dinucleotide bound to flavin reductase PCrystal structure of paprika ferredoxin-NADP+ reductase. Implications for the electron transfer pathwayProbing the determinants of coenzyme specificity in ferredoxin-NADP+ reductase by site-directed mutagenesisRole 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 ferredoxinProbing the role of glutamic acid 139 of Anabaena ferredoxin-NADP+ reductase in the interaction with substratesInvolvement of the pyrophosphate and the 2'-phosphate binding regions of ferredoxin-NADP+ reductase in coenzyme specificityCrystal structures of Leptospira interrogans FAD-containing ferredoxin-NADP+ reductase and its complex with NADP+X-ray Crystallographic and Solution State Nuclear Magnetic Resonance Spectroscopic Investigations of NADP + Binding to Ferredoxin NADP Reductase from Pseudomonas aeruginosa † , ‡Crystal structure analysis of Bacillus subtilis ferredoxin-NADP+ oxidoreductase and the structural basis for its substrate selectivityProbing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductaseA conserved aspartate (Asp-1393) regulates NADPH reduction of neuronal nitric-oxide synthase: implications for catalysisInvolvement of the flavin si-face tyrosine on the structure and function of ferredoxin-NADP+ reductases.The crystal structure of NADPH:ferredoxin reductase from Azotobacter vinelandiiModulation of the enzymatic efficiency of ferredoxin-NADP(H) reductase by the amino acid volume around the catalytic site.Flavin fluorescence dynamics and photoinduced electron transfer in Escherichia coli glutathione reductaseElectrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NADP+ reductase: site-specific mutagenesis, transient kinetic measurements, and electrostatic surface potentials.A conserved flavin-shielding residue regulates NO synthase electron transfer and nicotinamide coenzyme specificityOpen questions in ferredoxin-NADP+ reductase catalytic mechanism.Mechanism of Nitric Oxide Synthase Regulation: Electron Transfer and Interdomain Interactions.A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolutionCrystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogansNitric-oxide synthase (NOS) reductase domain models suggest a new control element in endothelial NOS that attenuates calmodulin-dependent activity.Interaction and electron transfer between ferredoxin-NADP(+) oxidoreductase and its partners: structural, functional, and physiological implications.Protein import into chloroplasts involves redox-regulated proteins.Cloning, expression, crystallization and preliminary X-ray studies of the ferredoxin-NAD(P)+ reductase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.Docking analysis of transient complexes: interaction of ferredoxin-NADP+ reductase with ferredoxin and flavodoxin.A redox-dependent interaction between two electron-transfer partners involved in photosynthesis.Thermal inactivation of reduced ferredoxin (flavodoxin):NADP+ oxidoreductase from Escherichia coli.The complete purification and characterization of three forms of ferredoxin-NADP(+) oxidoreductase from a thermophilic cyanobacterium Synechococcus elongatus.Small changes in the activity of chloroplastic NADP(+)-dependent ferredoxin oxidoreductase lead to impaired plant growth and restrict photosynthetic activity of transgenic tobacco plants.FAD is a preferred substrate and an inhibitor of Escherichia coli general NAD(P)H:flavin oxidoreductase.Inhibition of pea ferredoxin-NADP(H) reductase by Zn-ferrocyanide.Distinguishing two groups of flavin reductases by analyzing the protonation state of an active site carboxylic acid.Complex formation between Azotobacter vinelandii ferredoxin I and its physiological electron donor NADPH-ferredoxin reductase.Arabidopsis FNRL protein is an NADPH-dependent chloroplast oxidoreductase resembling bacterial ferredoxin-NADP+ reductases.The ferredoxin-binding site of ferredoxin: Nitrite oxidoreductase. Differential chemical modification of the free enzyme and its complex with ferredoxin.Competition between C-terminal Tyrosine and Nicotinamide Modulates Pyridine Nucleotide Affinity and Specificity in Plant Ferredoxin-NADP+Reductase
P2860
Q24652914-40BBCD9C-E82B-4FD2-9641-0C6AE5020575Q27619660-1F5CDB7A-87CF-44C6-A838-811CE9F911C8Q27627711-137747BE-2E3A-4837-844C-0C5D58272A3AQ27629226-26AFD865-B158-486A-82FE-21C9F886B15CQ27631672-FDAD58B9-F92A-4960-B1D6-D29F05111AA4Q27639835-AA6F23F1-738C-4995-BCB5-37DEDB46C060Q27642195-FBD0C863-1729-493F-BBF5-DAE2A1F350FCQ27648885-E308FA02-E0B9-4D64-B789-C19B50BD2E86Q27651048-EA16D80A-13A3-4D18-AC7E-60BEC6866E38Q27664733-ACB5A968-3281-4FB2-9E6F-D9524D48F23DQ27766345-EA1C1D19-52D0-4560-91FA-FD9225A867C1Q28577114-3556D569-081D-4CCC-B0FD-C7C6E10FAF84Q30167900-BE74511D-B7DC-4F34-BDC6-CF7C2E73C604Q30175930-F1E4AF8A-F5AE-485B-A0AE-635A4CFAFB57Q30367807-6F02A021-4D09-4B1C-AD68-58B2D5DC2EBEQ30430178-640FC16F-FA60-4C3B-ACA2-D5D384FCBCC8Q33178780-94E4B266-5E00-41C4-A729-B51983C31008Q34159837-78A62FAE-3A09-4437-9105-0A5B27AE880FQ34192164-8A937A99-66A3-4BBF-91E9-E997F4E13CC2Q34241528-E6EF7FBF-92F0-4421-BC89-AB4760189D3EQ36280273-14FB5ADC-7C59-4EC8-8159-117B04ABCF1EQ36459542-1E7E9501-B78F-4218-8994-363B4ADCAE84Q38353623-3217316E-F74B-4AA4-854B-0A0F2558C1D8Q39210413-D15F2237-C5F5-44B1-99E8-23C97F0AA416Q39687496-DCAFBDB3-8779-4C96-8505-5B62D88A55AEQ41993801-01D92EB4-16F6-4A37-BF71-FB30D28054C9Q42080846-7D252BEB-08E3-430E-91D8-E67C584F9AE0Q42111452-A94D12F9-790D-4CFA-9616-6C30AD57CA82Q42160661-7EEAB6AB-1396-4FE2-B5EA-EB8C88948399Q43030527-0FAE2AEB-6A73-473E-9F48-9D5A6DBB3805Q43885798-D044E5FB-E916-43CE-BE5E-B552B1A498A1Q44102186-5CB1980D-9036-4294-9DA5-E42C46A0DF99Q45160546-EFFB1AB4-2442-4F27-9EC1-2D83380913A9Q45946546-09CE6064-9128-413D-82B7-D64AC532D52FQ46106988-36C4C556-C602-45E0-BE7C-137A7D641CA3Q47764290-8248D187-1678-40F0-A0B6-339F7D1915DDQ48047881-98A15173-CEEF-4A03-9D7F-EE8019200E4BQ57971136-DCF0AC4D-40B0-4254-ACCB-235157859B1D
P2860
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
description
1996 nî lūn-bûn
@nan
1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@ast
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@en
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@nl
type
label
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@ast
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@en
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@nl
prefLabel
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@ast
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@en
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@nl
P2093
P356
P1476
X-ray structure of the ferredo ...... + binding at 2.25 A resolution
@en
P2093
Fontecilla-Camps JC
Gomez-Moreno C
Vellieux FM
P356
10.1006/JMBI.1996.0553
P407
P577
1996-10-01T00:00:00Z