Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S].

@article{Correll1992PhthalateDR,
  title={Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S].},
  author={Carl C. Correll and Christopher J. Batie and David P. Ballou and Martha Ludwig},
  journal={Science},
  year={1992},
  volume={258 5088},
  pages={
          1604-10
        }
}
Phthalate dioxygenase reductase (PDR) is a prototypical iron-sulfur flavoprotein (36 kilodaltons) that utilizes flavin mononucleotide (FMN) to mediate electron transfer from the two-electron donor, reduced nicotinamide adenine nucleotide (NADH), to the one-electron acceptor, [2Fe-2S]. The crystal structure of oxidized PDR from Pseudomonas cepacia has been analyzed at 2.0 angstrom resolution resolution; reduced PDR and pyridine nucleotide complexes have been analyzed at 2.7 angstrom resolution… 

Structure and mechanism of the iron‐sulfur flavoprotein phthalate dioxygenase reductase

TLDR
Kinetic studies have identified sequential steps in the reaction of PDR with NADH that involve pyridine nucleotide binding, hydrijde transfer to FMN, and intramolecular electron transfer from the reduced flavin to the [2Fe‐2S] cluster.

The NAD(P)H:Flavin Oxidoreductase from Escherichia coli

TLDR
It is shown that the flavin reductase selectively transfers the pro-R hydrogen from the C-4 position of the nicotinamide ring and is therefore classified as an A-side-specific enzyme.

Structural prototypes for an extended family of flavoprotein reductases: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin

TLDR
Hallmarks of this subfamily of flavoproteins, here termed the FNR family, are an antiparallel β‐barrel that binds the flavin prosthetic group, and a characteristic variant of the classic pyridine nucleotide‐binding fold.

Structure of T4moF, the Toluene 4-Monooxygenase Ferredoxin Oxidoreductase.

TLDR
The 1.6 Å crystal structure of toluene 4-monooxygenase reductase T4moF is reported and provides an excellent steric and electrostatic match to the obligate electron acceptor, Rieske-type [2Fe-2S] ferredoxin T 4moC.

Reaction of phthalate dioxygenase reductase with NADH and NAD: kinetic and spectral characterization of intermediates.

TLDR
The results of these analyses indicate that the reductive half-reaction of PDR consists of five distinct kinetic phases, which are surprising that this rate is so slow, since the shortest interatomic distance between these centers is only 4.7 A.

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.

TLDR
The results obtained with the homologous reductases from pea and Anabaena PCC7119 indicate that interactions with Fd or Fld are hardly affected by replacement of this tyrosine by tryptophan, phenylalanine, or serine, without major differences between the eukaryotic and the bacterial FNR.
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TLDR
Conclusive evidence is presented that the ferredoxin reductase structure is a prototype for the nicotinamide dinucleotide and FAD binding domains of the enzymes NADPH-cytochrome P450 reduct enzyme, NAD PH-sulfite reductases, NADH-cy tochrome b5 reductasing enzymes, and NADh-nitrate reduCTase.

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TLDR
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TLDR
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TLDR
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