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 L. 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… Expand
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. Expand
X-ray crystal structure of benzoate 1,2-dioxygenase reductase from Acinetobacter sp. strain ADP1.
TLDR
The BenC structure is the first determined for a reductase from the class IB Rieske dioxygenases, whose reductases transfer electrons directly to their oxygenase components. Expand
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. Expand
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. Expand
Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.
TLDR
The close proximity of the three redox centers makes it possible to propose a possible electron transfer pathway involving residues conserved among the family 1B DHODs. Expand
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. Expand
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. Expand
2-oxo-1,2-dihydroquinoline 8-monooxygenase: phylogenetic relationship to other multicomponent nonheme iron oxygenases
2-Oxo-1,2-dihydroquinoline 8-monooxygenase, an enzyme involved in quinoline degradation by Pseudomonas putida 86, had been identified as a class IB two-component nonheme iron oxygenase based on itsExpand
Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida.
TLDR
Structural analysis showed that in reduced Pdx the Cys45-Ala46 peptide bond flip initiates readjustment of hydrogen bonding interactions between the [2Fe-2S] cluster, the Sgamma atoms of the cysteinyl ligands, and the backbone amide nitrogen atoms that results in tightening of the metal cluster binding loop around the prosthetic group. Expand
The 2Fe2S centres of the 2-oxo-1,2-dihydroquinoline 8-monooxygenase from Pseudomonas putida 86 studied by EPR spectroscopy.
TLDR
An EPR characterization of the iron-sulfur centres in the purified reductase and oxygenase component of this novel enzyme system and a detailed comparison to other multicomponent enzyme systems is presented pointing out the EPR and redox properties of the FeS centres involved. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 56 REFERENCES
Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomonas cepacia.
TLDR
The phthalate oxygenase reductase induced in Pseudomonas cepacia is a single polypeptide chain with two prosthetic groups, FMN and [2Fe-2S], which has been crystallized at pH 6.7 from polyethylene glycol 6000 in space group R3. Expand
Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family.
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. Expand
Three-dimensional structure of the iron-sulfur flavoprotein trimethylamine dehydrogenase at 2.4-A resolution.
TLDR
The three-dimensional structure of trimethylamine dehydrogenase from the methylotrophic bacterium W3A1 has been determined to 2.4-A resolution and the topologies and spatial arrangements of these two domains are remarkably similar to the FAD- and NADPH-binding domains of glutathione reductase. Expand
Reconstitution of iron-sulfur cluster of NADH-cytochrome c reductase, a component of benzoate 1,2-dioxygenase system from Pseudomonas arvilla C-1.
TLDR
Although the iron-sulfur-depleted enzyme catalyzed NADH-dependent reduction of ferricyanide, nitroblue tetrazolium, or oxygen, it could not catalyze NADH/NADH- dependent reduction of the oxygenase component of benzoate 1,2-dioxygenase system, and the reconstituted enzyme recovered the activity of NADH’s role in reducing oxygen to the original level. Expand
Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia.
An enzymatic system has been isolated that catalyzes dihydroxylation of phthalate to form 1,2-dihydroxy-4,5-dicarboxy-3,5-cyclohexadiene with consumption of NADH and O2. This system is comprised ofExpand
Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0-A resolution.
TLDR
The course of the polypeptide chain of the flavoprotein subunit, whose sequence is mostly unknown, has been traced in a minimap and a model of polyalanine fitted to the electron density on the graphics system. Expand
Comparison of the kinetics of reduction and intramolecular electron transfer in electrostatic and covalent complexes of ferredoxin-NADP+ reductase and flavodoxin from Anabaena PCC 7119.
The kinetics of reduction and intracomplex electron transfer in electrostatically stabilized and covalently crosslinked complexes between ferredoxin-NADP+ reductase (FNR) and flavodoxin (Fld) fromExpand
Electron-nuclear double resonance spectroscopy of 15N-enriched phthalate dioxygenase from Pseudomonas cepacia proves that two histidines are coordinated to the [2Fe-2S] Rieske-type clusters.
TLDR
The structure deduced here for the PDO cluster is generally applicable to the full class of Rieske-type centers and the bonding parameters of the coordinated nitrogens are fully consistent with those of an spn hybrid on a histidyl nitrogen coordinated to Fe. Expand
Electron transfer reactions in the soluble methane monooxygenase of Methylococcus capsulatus (Bath).
TLDR
Aerobic stopped-flow experiments have confirmed that component C is the methane monooxygenase component responsible for interaction with NADH, and removal and reconstitution of the redox centres of component C suggest a correlation between the presence of the FAD and Fe2S2Redox centres and NADH: acceptor reductase activity and methane mono Oxygenase activity respectively, consistent with the order of electron flow. Expand
Nucleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases.
TLDR
Comparison of the deduced amino acid sequences of BenABC with related sequences, including those for the multicomponent toluate, toluene, benzene, and naphthalene 1,2-dioxygenases, indicated that the similarly sized subunits of the hydroxylase components were derived from a common ancestor. Expand
...
1
2
3
4
5
...