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A redox‐dependent interaction between two electron‐transfer partners involved in photosynthesis
TLDR
The interaction between oxidized FNR and Fd was studied by crystallography at 2.4 Å resolution leading to a three‐dimensional picture of an Fd–FNR biologically relevant complex, which suggests that FNRand Fd specifically interact prior to each electron transfer and disassemble upon a redox‐linked conformational change of the Fd. Expand
Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials.
TLDR
Comparison of the binding energies of wild-type and mutant flavodoxins at the three redox states suggests that the interaction between Tyr94 and FMN stabilizes the apoflavodoxin--FMN complex in all redoxStates, and suggests that Trp57 could play a role in the kinetics of flavodoxin redox reactions. Expand
Ferredoxin-dependent photosynthetic reduction of nitrate and nitrite by particles of anacystis nidulans
TLDR
In its presence, the alga particles catalyze the gradual photoreduction of nitrate to nitrite and ammonia, a process that can thus be considered as one of the most simple and relevant examples of Photosynthesis. Expand
Interaction of Ferredoxin–NADP+ Reductase with its Substrates: Optimal Interaction for Efficient Electron Transfer
TLDR
The present manuscript summarises the information so far reported for an efficient interaction between F NR and its substrates, compares such information with that revealed by other systems for which the FNR structure is a prototype, and discusses the implications of the processes of association in ET between FNR and its substrateates. Expand
Flavoenzyme-catalyzed redox cycling of hydroxylamino- and amino metabolites of 2,4,6-trinitrotoluene: implications for their cytotoxicity.
TLDR
The data imply that the flavoenzyme-catalyzed redox cycling of amino and hydroxylamino metabolites of TNT may be an important factor in their cytotoxicity, and increased with an increase in their electron accepting properties, or their reactivity towards the single-electron transferring FNR and P-450R. Expand
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.
TLDR
The crystal structure of the ferredoxin:NADP+ reductase (FNR) from the cyanobacterium Anabaena PCC 7119 has been determined and the model of the complex agrees with previous biochemical studies as residues Arg 100 and Arg 233 are involved in NADP+ binding and residues Arg77, Lys 53 and Lys 294, located on the FAD side of the enzyme, remain free to interact with fer redoxin and flavodoxin. Expand
Electrostatic forces involved in orienting Anabaena ferredoxin during binding to Anabaena ferredoxin:NAdp+ reductase: Site‐specific mutagenesis, transient kinetic measurements, and electrostatic
TLDR
The relative changes in et kinetics and complex binding constants for these mutants are attributed to these characteristics of the surface charge distribution in FNR and conclude that the positively charged region of the FNR surface located in the vicinity of K75, R16, and K72 is especially important in the binding and orientation of Fd during electron transfer. Expand
Involvement of the Pyrophosphate and the 2′-Phosphate Binding Regions of Ferredoxin-NADP+ Reductase in Coenzyme Specificity*
TLDR
The results confirm that determinants for coenzyme specificity in FNR are also situated in the pyrophosphate binding region and not only in the 2′-P binding region, and suggest that other regions of the protein, yet to be identified, might also be involved in this process. Expand
Involvement of glutamic acid 301 in the catalytic mechanism of ferredoxin-NADP+ reductase from Anabaena PCC 7119.
TLDR
Fast transient kinetic studies corroborated that removal of the carboxylate at position 301 decreases the rate constant for the electron transfer process with ferredoxin without appreciably affecting complex formation, and thus interferes with the stabilization of the transition state during electron-transfer between the FAD and the iron-sulfur cluster. Expand
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
TLDR
It is concluded that nonconservative mutations of three critical residues (S47, F65, and E94) on the surface of ferredoxin have large parallel effects on both the reduction potential and the electron-transfer reactivity of the [2Fe-2S] cluster, thereby making electron transfer thermodynamically feasible. Expand
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