The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
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[1] Mi Hee Lim,et al. Structural insights into nonheme alkylperoxoiron(III) and oxoiron(IV) intermediates by X-ray absorption spectroscopy. , 2004, Journal of the American Chemical Society.
[2] P. Siegbahn,et al. Quantum chemical studies of dioxygen activation by mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad. , 2004, Dalton transactions.
[3] C. Schofield,et al. Crystal structure and mechanistic implications of 1-aminocyclopropane-1-carboxylic acid oxidase--the ethylene-forming enzyme. , 2004, Chemistry & biology.
[4] L. Que,et al. Oxygenase activity in the self-hydroxylation of (s)-2-hydroxypropylphosphonic acid epoxidase involved in fosfomycin biosynthesis. , 2004, Journal of the American Chemical Society.
[5] P. Siegbahn,et al. Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases. , 2004, Journal of the American Chemical Society.
[6] Carsten Krebs,et al. EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase. , 2004, Journal of the American Chemical Society.
[7] E. Solomon,et al. Spectroscopic and Quantum Chemical Characterization of the Electronic Structure and Bonding in a Non-Heme FeIVO Complex , 2004 .
[8] M. Blomberg,et al. A theoretical study of the cis-dihydroxylation mechanism in naphthalene 1,2-dioxygenase , 2004, JBIC Journal of Biological Inorganic Chemistry.
[9] L. Que,et al. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates. , 2004, Chemical reviews.
[10] L. Que,et al. Nonheme FeIVO complexes that can oxidize the C-H bonds of cyclohexane at room temperature. , 2004, Journal of the American Chemical Society.
[11] M. J. Ryle,et al. Direct detection of oxygen intermediates in the non-heme Fe enzyme taurine/alpha-ketoglutarate dioxygenase. , 2004, Journal of the American Chemical Society.
[12] Robert P. Hausinger,et al. Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes , 2004 .
[13] D. Mansuy,et al. Spectroscopic Characterization of an FeIV Intermediate Generated by Reaction of XO− (X = Cl, Br) with an FeII Complex Bearing a Pentadentate Non-Porphyrinic Ligand − Hydroxylation and Epoxidation Activity , 2004 .
[14] J. Hajdu,et al. The structural basis of cephalosporin formation in a mononuclear ferrous enzyme , 2004, Nature Structural &Molecular Biology.
[15] L. Que,et al. Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: single turnover reaction , 2004, JBIC Journal of Biological Inorganic Chemistry.
[16] P. Fitzpatrick. Mechanism of aromatic amino acid hydroxylation. , 2003, Biochemistry.
[17] J. Lipscomb,et al. Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme. , 2003, Biochemistry.
[18] Carsten Krebs,et al. Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:alpha-ketoglutarate dioxygenase (TauD). , 2003, Journal of the American Chemical Society.
[19] T. Bugg. Dioxygenase Enzymes: Catalytic Mechanisms and Chemical Models , 2003 .
[20] L. Que,et al. A dramatic push effect on the homolysis of FeIII(OOR) intermediates to form non-heme FeIV=O complexes. , 2003, Angewandte Chemie.
[21] Carsten Krebs,et al. The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase: a high-spin FeIV complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli. , 2003, Biochemistry.
[22] M. Costas,et al. An FeIVO complex of a tetradentate tripodal nonheme ligand , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[23] N. Lehnert,et al. Non-heme iron enzymes: Contrasts to heme catalysis , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[24] H. Eklund,et al. Crystal Structure of Naphthalene Dioxygenase: Side-on Binding of Dioxygen to Iron , 2003, Science.
[25] Mi Hee Lim,et al. Crystallographic and spectroscopic characterization of a nonheme Fe(IV)-O complex. , 2003, Science.
[26] T. Bugg,et al. A density functional investigation of the extradiol cleavage mechanism in non-heme iron catechol dioxygenases , 2003, JBIC Journal of Biological Inorganic Chemistry.
[27] L. Wackett. Mechanism and applications of Rieske non-heme iron dioxygenases , 2002 .
[28] T. Nonaka,et al. Crystal structures of the reaction intermediate and its homologue of an extradiol-cleaving catecholic dioxygenase. , 2002, Journal of molecular biology.
[29] R. Stevens,et al. Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates. , 2002, Journal of molecular biology.
[30] L. Que,et al. Spectroscopic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: molecular mechanism and CO(2) activation in the biosynthesis of ethylene. , 2002, Journal of the American Chemical Society.
[31] Christopher J Schofield,et al. Crystal structure of a clavaminate synthase–Fe(II)–2‐oxoglutarate–substrate–NO complex: evidence for metal centred rearrangements , 2002, FEBS letters.
[32] D. Timm,et al. Crystal structure of human homogentisate dioxygenase , 2000, Nature Structural Biology.
[33] Lawrence Que,et al. One motif — many different reactions , 2000, Nature Structural Biology.
[34] Christopher J. Schofield,et al. Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase , 2000, Nature Structural Biology.
[35] Mindy I. Davis,et al. Geometric and electronic structure/function correlations in non-heme iron enzymes. , 2000, Chemical reviews.
[36] C. Schofield,et al. Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes. , 1999, Current opinion in structural biology.
[37] L. Serre,et al. Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway. , 1999, Structure.
[38] M. Fukuda,et al. Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions. , 1999, Structure.
[39] R. Stevens,et al. Structural Insight into the Aromatic Amino Acid Hydroxylases and Their Disease-Related Mutant Forms. , 1999, Chemical reviews.
[40] R. Christoffersen,et al. Role of the nonheme Fe(II) center in the biosynthesis of the plant hormone ethylene. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[41] R. Stevens,et al. Structural basis of autoregulation of phenylalanine hydroxylase , 1999, Nature Structural Biology.
[42] M. D. Lloyd,et al. Structure of a cephalosporin synthase , 1998, Nature.
[43] D T Gibson,et al. Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase. , 1998, Structure.
[44] J. Hajdu,et al. Proteins of the penicillin biosynthesis pathway. , 1997, Current opinion in structural biology.
[45] L. Que,et al. The 2-His-1-carboxylate facial triad--an emerging structural motif in mononuclear non-heme iron(II) enzymes. , 1997, European journal of biochemistry.
[46] Raymond C. Stevens,et al. Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases , 1997, Nature Structural Biology.
[47] J. Hajdu,et al. Structure of isopenicillinN synthase complexed with substrate and the mechanism ofpenicillin formation , 1997, Nature.
[48] T. J. Kappock,et al. Pterin-Dependent Amino Acid Hydroxylases. , 1996, Chemical reviews.
[49] J. Dawson,et al. Heme-Containing Oxygenases. , 1996, Chemical reviews.
[50] J. Bolin,et al. Evolutionary relationships among extradiol dioxygenases , 1996, Journal of bacteriology.
[51] T. Bugg,et al. Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases , 1996, Journal of bacteriology.
[52] D. Gibson,et al. Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sites , 1996, Journal of bacteriology.
[53] I. Borovok,et al. Ferrous active site of isopenicillin N synthase: genetic and sequence analysis of the endogenous ligands. , 1996, Biochemistry.
[54] M. Fukuda,et al. Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102. , 1996, Journal of molecular biology.
[55] T. Sim,et al. Functional Analysis of Conserved Histidine Residues in Cephalosporium acremonium Isopenicillin N Synthase by Site-directed Mutagenesis (*) , 1996, The Journal of Biological Chemistry.
[56] Q. Jiang,et al. Ruthenium‐Catalyzed cis‐Dihydroxylation of Alkenes: Scope and Limitations , 1996 .
[57] J. Bolin,et al. Crystal Structure of the Biphenyl-Cleaving Extradiol Dioxygenase from a PCB-Degrading Pseudomonad , 1995, Science.
[58] Geoffrey J. Barton,et al. Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes , 1995, Nature.
[59] A. Prescott. A Dilemma of Dioxygenases (or Where Biochemistry and Molecular Biology Fail to Meet) , 1993 .
[60] Donald G. Lee,et al. Oxidation of hydrocarbons. 18. Mechanism of the reaction between permanganate and carbon-carbon double bonds , 1989 .
[61] M. Schroeder. Osmium tetraoxide cis hydroxylation of unsaturated substrates , 1980 .