Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 4 December 1992:
Vol. 258. no. 5088, pp. 1604 - 1610
DOI: 10.1126/science.1280857
Prev | Table of Contents | Next

Articles

Science, Vol 258, Issue 5088, 1604-1610
Copyright © 1992 by American Association for the Advancement of Science

articles

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

CC Correll, CJ Batie, DP Ballou, and ML Ludwig

Department of Biological Chemistry and Biophysics, University of Michigan, Ann Arbor 48109.

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. NADH, FMN, and the [2Fe-2S] cluster, bound to distinct domains, are brought together near a central cleft in the molecule, with only 4.9 angstroms separating the flavin 8-methyl and a cysteine sulfur ligated to iron. The domains that bind FMN and [2Fe-2S] are packed so that the flavin ring and the plane of the [2Fe-2S] core are approximately perpendicular. The [2Fe-2S] group is bound by four cysteines in a site resembling that in plant ferredoxins, but its redox potential (-174 millivolts at pH 7.0) is much higher than the potentials of plant ferredoxins. Structural and sequence similarities assign PDR to a distinct family of flavoprotein reductases, all related to ferredoxin NADP(+)-reductase.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Purine Utilization by Klebsiella oxytoca M5al: Genes for Ring-Oxidizing and -Opening Enzymes.
S. D. Pope, L.-L. Chen, and V. Stewart (2009)
J. Bacteriol. 191, 1006-1017
   Abstract »    Full Text »    PDF »
Characterization of a Second Rhodococcus erythropolis SQ1 3-Ketosteroid 9{alpha}-Hydroxylase Activity Comprising a Terminal Oxygenase Homologue, KshA2, Active with Oxygenase-Reductase Component KshB.
R. van der Geize, G. I. Hessels, M. Nienhuis-Kuiper, and L. Dijkhuizen (2008)
Appl. Envir. Microbiol. 74, 7197-7203
   Abstract »    Full Text »    PDF »
Novel {beta}-Barrel Fold in the Nuclear Magnetic Resonance Structure of the Replicase Nonstructural Protein 1 from the Severe Acute Respiratory Syndrome Coronavirus.
M. S. Almeida, M. A. Johnson, T. Herrmann, M. Geralt, and K. Wuthrich (2007)
J. Virol. 81, 3151-3161
   Abstract »    Full Text »    PDF »
Domain Engineering of the Reductase Component of Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath).
J. L. Blazyk and S. J. Lippard (2004)
J. Biol. Chem. 279, 5630-5640
   Abstract »    Full Text »    PDF »
A Self-sufficient Cytochrome P450 with a Primary Structural Organization That Includes a Flavin Domain and a [2Fe-2S] Redox Center.
G. A. Roberts, A. Celik, D. J. B. Hunter, T. W. B. Ost, J. H. White, S. K. Chapman, N. J. Turner, and S. L. Flitsch (2003)
J. Biol. Chem. 278, 48914-48920
   Abstract »    Full Text »    PDF »
Involvement of the Pyrophosphate and the 2'-Phosphate Binding Regions of Ferredoxin-NADP+ Reductase in Coenzyme Specificity.
J. Tejero, M. Martinez-Julvez, T. Mayoral, A. Luquita, J. Sanz-Aparicio, J. A. Hermoso, J. K. Hurley, G. Tollin, C. Gomez-Moreno, and M. Medina (2003)
J. Biol. Chem. 278, 49203-49214
   Abstract »    Full Text »    PDF »
Structural Features of Covalently Cross-linked Hydroxylase and Reductase Proteins of Soluble Methane Monooxygenase as Revealed by Mass Spectrometric Analysis.
D. A. Kopp, E. A. Berg, C. E. Costello, and S. J. Lippard (2003)
J. Biol. Chem. 278, 20939-20945
   Abstract »    Full Text »    PDF »
Role of Thr66 in Porcine NADH-cytochrome b5 Reductase in Catalysis and Control of the Rate-limiting Step in Electron Transfer.
S. Kimura, M. Kawamura, and T. Iyanagi (2003)
J. Biol. Chem. 278, 3580-3589
   Abstract »    Full Text »    PDF »
A Previously Unrecognized Step in Pentachlorophenol Degradation in Sphingobium chlorophenolicum Is Catalyzed by Tetrachlorobenzoquinone Reductase (PcpD).
M. Dai, J. B. Rogers, J. R. Warner, and S. D. Copley (2003)
J. Bacteriol. 185, 302-310
   Abstract »    Full Text »    PDF »
Purification and Characterization of Carbazole 1,9a-Dioxygenase, a Three-Component Dioxygenase System of Pseudomonas resinovorans Strain CA10.
J.-W. Nam, H. Nojiri, H. Noguchi, H. Uchimura, T. Yoshida, H. Habe, H. Yamane, and T. Omori (2002)
Appl. Envir. Microbiol. 68, 5882-5890
   Abstract »    Full Text »    PDF »
Identification of a New Class of Cytochrome P450 from a Rhodococcus sp..
G. A. Roberts, G. Grogan, A. Greter, S. L. Flitsch, and N. J. Turner (2002)
J. Bacteriol. 184, 3898-3908
   Abstract »    Full Text »    PDF »
Biodegradation of Aromatic Compounds by Escherichia coli.
E. Diaz, A. Ferrandez, M. A. Prieto, and J. L. Garcia (2001)
Microbiol. Mol. Biol. Rev. 65, 523-569
   Abstract »    Full Text »    PDF »
Genetic Characterization and Evolutionary Implications of a car Gene Cluster in the Carbazole Degrader Pseudomonas sp. Strain CA10.
H. Nojiri, H. Sekiguchi, K. Maeda, M. Urata, S.-I. Nakai, T. Yoshida, H. Habe, and T. Omori (2001)
J. Bacteriol. 183, 3663-3679
   Abstract »    Full Text »
Identification of Methyl Halide-Utilizing Genes in the Methyl Bromide-Utilizing Bacterial Strain IMB-1 Suggests a High Degree of Conservation of Methyl Halide-Specific Genes in Gram-Negative Bacteria.
C. A. Woodall, K. L. Warner, R. S. Oremland, J. C. Murrell, and I. R. McDonald (2001)
Appl. Envir. Microbiol. 67, 1959-1963
   Abstract »    Full Text »
Engineering of a functional human NADH-dependent cytochrome P450 system.
O. Dohr, M. J. I. Paine, T. Friedberg, G. C. K. Roberts, and C. R. Wolf (2001)
PNAS 98, 81-86
   Abstract »    Full Text »    PDF »
Substrate Range and Genetic Analysis of Acinetobacter Vanillate Demethylase.
B. Morawski, A. Segura, and L. N. Ornston (2000)
J. Bacteriol. 182, 1383-1389
   Abstract »    Full Text »
Soluble Methane Monooxygenase Gene Clusters from Trichloroethylene-Degrading Methylomonas sp. Strains and Detection of Methanotrophs during In Situ Bioremediation.
T. Shigematsu, S. Hanada, M. Eguchi, Y. Kamagata, T. Kanagawa, and R. Kurane (1999)
Appl. Envir. Microbiol. 65, 5198-5206
   Abstract »    Full Text »
Characterization of the Phthalate Permease OphD from Burkholderia cepacia ATCC 17616.
H.-K. Chang and G. J. Zylstra (1999)
J. Bacteriol. 181, 6197-6199
   Abstract »    Full Text »
Identification of an NADH-Cytochrome b5 Reductase Gene from an Arachidonic Acid-Producing Fungus, Mortierella alpina 1S-4, by Sequencing of the Encoding cDNA and Heterologous Expression in a Fungus, Aspergillus oryzae.
E. Sakuradani, M. Kobayashi, and S. Shimizu (1999)
Appl. Envir. Microbiol. 65, 3873-3879
   Abstract »    Full Text »
The NAD(P)H:Flavin Oxidoreductase from Escherichia coli. EVIDENCE FOR A NEW MODE OF BINDING FOR REDUCED PYRIDINE NUCLEOTIDES.
V. Niviere, F. Fieschi, J.-L. Decout, and M. Fontecave (1999)
J. Biol. Chem. 274, 18252-18260
   Abstract »    Full Text »    PDF »
Genetic Analysis of a Chromosomal Region Containing vanA and vanB, Genes Required for Conversion of Either Ferulate or Vanillate to Protocatechuate in Acinetobacter.
A. Segura, P. V. Bünz, D. A. D'Argenio, and L. N. Ornston (1999)
J. Bacteriol. 181, 3494-3504
   Abstract »    Full Text »
Novel Organization of the Genes for Phthalate Degradation from Burkholderia cepacia DBO1.
H.-K. Chang and G. J. Zylstra (1998)
J. Bacteriol. 180, 6529-6537
   Abstract »    Full Text »
Catabolism of Phenylacetic Acid in Escherichia coli. CHARACTERIZATION OF A NEW AEROBIC HYBRID PATHWAY.
A. Ferrandez, B. Minambres, B. Garcia, E. R. Olivera, J. M. Luengo, J. L. Garcia, and E. Diaz (1998)
J. Biol. Chem. 273, 25974-25986
   Abstract »    Full Text »    PDF »
Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes.
M. Wang, D. L. Roberts, R. Paschke, T. M. Shea, B. S. S. Masters, and J.-J. P. Kim (1997)
PNAS 94, 8411-8416
   Abstract »    Full Text »    PDF »
Is the NAD(P)H:Flavin Oxidoreductase from Escherichia coli a Member of the Ferredoxin-NADP+ Reductase Family?. EVIDENCE FOR THE CATALYTIC ROLE OF SERINE 49RESIDUE.
V. Niviere, F. Fieschi, J.-L. Decout, and M. Fontecave (1996)
J. Biol. Chem. 271, 16656-16661
   Abstract »    Full Text »    PDF »
The Role of Threonine 54 in Adrenodoxin for the Properties of Its Iron-Sulfur Cluster and Its Electron Transfer Function.
H. Uhlmann and R. Bernhardt (1995)
J. Biol. Chem. 270, 29959-29966
   Abstract »    Full Text »    PDF »
Spectroscopic and Kinetic Characterization of the Recombinant Wild-type and C242S Mutant of the Cytochrome b Reductase Fragment of Nitrate Reductase.
K. Ratnam, N. Shiraishi, W. H. Campbell, and R. Hille (1995)
J. Biol. Chem. 270, 24067-24072
   Abstract »    Full Text »    PDF »
Ferredoxin-dependent Redox System of a Thermoacidophilic Archaeon, Sulfolobus sp. Strain 7.
T. Iwasaki, T. Wakagi, and T. Oshima (1995)
J. Biol. Chem. 270, 17878-17883
   Abstract »    Full Text »    PDF »
Crystal Structure of Paprika Ferredoxin-NADP+ Reductase. IMPLICATIONS FOR THE ELECTRON TRANSFER PATHWAY.
A. Dorowski, A. Hofmann, C. Steegborn, M. Boicu, and R. Huber (2001)
J. Biol. Chem. 276, 9253-9263
   Abstract »    Full Text »    PDF »
Probing the Determinants of Coenzyme Specificity in Ferredoxin-NADP+ Reductase by Site-directed Mutagenesis.
M. Medina, A. Luquita, J. Tejero, J. Hermoso, T. Mayoral, J. Sanz-Aparicio, K. Grever, and C. Gomez-Moreno (2001)
J. Biol. Chem. 276, 11902-11912
   Abstract »    Full Text »    PDF »
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.
M. Martinez-Julvez, I. Nogues, M. Faro, J. K. Hurley, T. B. Brodie, T. Mayoral, J. Sanz-Aparicio, J. A. Hermoso, M. T. Stankovich, M. Medina, et al. (2001)
J. Biol. Chem. 276, 27498-27510
   Abstract »    Full Text »    PDF »
Crystal Structure of the FAD/NADPH-binding Domain of Rat Neuronal Nitric-oxide Synthase. COMPARISONS WITH NADPH-CYTOCHROME P450 OXIDOREDUCTASE.
J. Zhang, P. Martasek, R. Paschke, T. Shea, B. S. Siler Masters, and J.-J. P. Kim (2001)
J. Biol. Chem. 276, 37506-37513
   Abstract »    Full Text »    PDF »
Involvement of the Flavin si-Face Tyrosine on the Structure and Function of Ferredoxin-NADP+ Reductases.
A. K. Arakaki, E. G. Orellano, N. B. Calcaterra, J. Ottado, and E. A. Ceccarelli (2001)
J. Biol. Chem. 276, 44419-44426
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)