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Science 22 April 1988:
Vol. 240. no. 4851, pp. 433 - 439
DOI: 10.1126/science.3358128
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Articles

Science, Vol 240, Issue 4851, 433-439
Copyright © 1988 by American Association for the Advancement of Science

articles

Probing structure-function relations in heme-containing oxygenases and peroxidases

JH Dawson

Department of Chemistry, University of South Carolina, Columbia 29208.

Structural factors that influence functional properties are examined in the case of four heme enzymes: cytochrome P-450, chloroperoxidase, horseradish peroxidase, and secondary amine mono-oxygenase. The identity of the axial ligand, the nature of the heme environment, and the steric accessibility of the heme iron and heme edge combine to play major roles in determining the reactivity of each enzyme. The importance of synthetic porphyrin models in understanding the properties of the protein-free metal center is emphasized. The conclusions described herein have been derived from studies at the interface between biological and inorganic chemistry.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine.
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Axial ligand tuning of a nonheme iron(IV) oxo unit for hydrogen atom abstraction.
C. V. Sastri, J. Lee, K. Oh, Y. J. Lee, J. Lee, T. A. Jackson, K. Ray, H. Hirao, W. Shin, J. A. Halfen, et al. (2007)
PNAS 104, 19181-19186
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Heme Induces Neutrophil Migration and Reactive Oxygen Species Generation through Signaling Pathways Characteristic of Chemotactic Receptors.
B. N. Porto, L. S. Alves, P. L. Fernandez, T. P. Dutra, R. T. Figueiredo, A. V. Graca-Souza, and M. T. Bozza (2007)
J. Biol. Chem. 282, 24430-24436
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Prostaglandin Endoperoxide H Synthases: PEROXIDASE HYDROPEROXIDE SPECIFICITY AND CYCLOOXYGENASE ACTIVATION.
J. Liu, S. A. Seibold, C. J. Rieke, I. Song, R. I. Cukier, and W. L. Smith (2007)
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A Symbiotic Plant Peroxidase Involved in Bacterial Invasion of the Tropical Legume Sesbania rostrata.
J. Den Herder, S. Lievens, S. Rombauts, M. Holsters, and S. Goormachtig (2007)
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Structure and Reactivity of a Thermostable Prokaryotic Nitric-oxide Synthase That Forms a Long-lived Oxy-Heme Complex.
J. Sudhamsu and B. R. Crane (2006)
J. Biol. Chem. 281, 9623-9632
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Direct Observation of a Novel Perturbed Oxyferrous Catalytic Intermediate during Reduced Putidaredoxin-initiated Turnover of Cytochrome P-450-CAM: PROBING THE EFFECTOR ROLE OF PUTIDAREDOXIN IN CATALYSIS.
M. C. Glascock, D. P. Ballou, and J. H. Dawson (2005)
J. Biol. Chem. 280, 42134-42141
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Selective Perturbation of the Intravesicular Heme Center of Cytochrome b561 by Cysteinyl Modification with 4,4'-Dithiodipyridine.
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J. Biochem. 138, 751-762
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X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry.
K. L. Stone, R. K. Behan, and M. T. Green (2005)
PNAS 102, 16563-16565
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Reaction of Ferric Cytochrome P450cam with Peracids: KINETIC CHARACTERIZATION OF INTERMEDIATES ON THE REACTION PATHWAY.
T. Spolitak, J. H. Dawson, and D. P. Ballou (2005)
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Identification and Characterization of a Novel Vitamin B12 (Cobalamin) Biosynthetic Enzyme (CobZ) from Rhodobacter capsulatus, Containing Flavin, Heme, and Fe-S Cofactors.
H. M. McGoldrick, C. A. Roessner, E. Raux, A. D. Lawrence, K. J. McLean, A. W. Munro, S. Santabarbara, S. E. J. Rigby, P. Heathcote, A. I. Scott, et al. (2005)
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NMR Study on the Structural Changes of Cytochrome P450cam upon the Complex Formation with Putidaredoxin: FUNCTIONAL SIGNIFICANCE OF THE PUTIDAREDOXIN-INDUCED STRUCTURAL CHANGES.
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Pharmacol. Rev. 55, 551-571
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Direct Detection of Fe(IV)=O Intermediates in the Cytochrome aa3 Oxidase from Paracoccus denitrificans/H2O2 Reaction.
E. Pinakoulaki, U. Pfitzner, B. Ludwig, and C. Varotsis (2003)
J. Biol. Chem. 278, 18761-18766
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Bioinorganic Chemistry Special Feature: Neutral thiol as a proximal ligand to ferrous heme iron: Implications for heme proteins that lose cysteine thiolate ligation on reduction.
R. Perera, M. Sono, J. A. Sigman, T. D. Pfister, Y. Lu, and J. H. Dawson (2003)
PNAS 100, 3641-3646
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Two-dimensional NMR Study of the Heme Active Site Structure of Chloroperoxidase.
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Verapamil Metabolism in Distinct Regions of the Heart and in Cultures of Cardiomyocytes of Adult Rats.
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A Tomato Peroxidase Involved in the Synthesis of Lignin and Suberin.
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X. Yi, M. Mroczko, K. M. Manoj, X. Wang, and L. P. Hager (1999)
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An Unusual Dehalogenating Peroxidase from the Marine Terebellid Polychaete Amphitrite ornata.
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Uncoupling Oxygen Transfer and Electron Transfer in the Oxygenation of Camphor Analogues by Cytochrome P450-CAM.
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Alteration of Axial Coordination by Protein Engineering in Myoglobin.
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X-ray Absorption Near Edge Studies of Cytochrome P-450-CAM, Chloroperoxidase, and Myoglobin.
H. I. Liu, M. Sono, S. Kadkhodayan, L. P. Hager, B. Hedman, K. O. Hodgson, and J. H. Dawson (1995)
J. Biol. Chem. 270, 10544-10550
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Heme Oxygenase-2.
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J. Biol. Chem. 270, 6345-6350
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Characteristics of the Nitric Oxide Synthase-catalyzed Conversion of Arginine to N-Hydroxyarginine, the First Oxygenation Step in the Enzymic Synthesis of Nitric Oxide.
K. L. Campos, J. Giovanelli, and S. Kaufman (1995)
J. Biol. Chem. 270, 1721-1728
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Mechanism of catalytic oxygenation of alkanes by halogenated iron porphyrins.
M. Grinstaff, M. Hill, J. Labinger, and H. Gray (1994)
Science 264, 1311-1313
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Metalloenzymes, structural motifs, and inorganic models.
K. Karlin (1993)
Science 261, 701-708
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Oxygen activation at the diiron center of ribonucleotide reductase.
L Que Jr (1991)
Science 253, 273-274
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Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES.
M Sivaraja, D. Goodin, M Smith, and B. Hoffman (1989)
Science 245, 738-740
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The Crystal Structure and Amino Acid Sequence of Dehaloperoxidase from Amphitrite ornata Indicate Common Ancestry with Globins.
M. W. LaCount, E. Zhang, Y. P. Chen, K. Han, M. M. Whitton, D. E. Lincoln, S. A. Woodin, and L. Lebioda (2000)
J. Biol. Chem. 275, 18712-18716
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Flavohemoglobin, a Globin with a Peroxidase-like Catalytic Site.
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