| scholarly article | Q13442814 |
| P50 | author | John D. Lipscomb | Q38327124 |
| P2093 | author name string | John D Lipscomb | |
| P2860 | cites work | Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane | Q22061879 |
| Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling | Q27618123 | ||
| Crystal Structures of Fe2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates | Q27644520 | ||
| Intermediate in the O−O Bond Cleavage Reaction of an Extradiol Dioxygenase † , ‡ | Q27652335 | ||
| Structural Basis for the Role of Tyrosine 257 of Homoprotocatechuate 2,3-Dioxygenase in Substrate and Oxygen Activation | Q27674540 | ||
| Visualizing the substrate-, superoxo-, alkylperoxo-, and product-bound states at the nonheme Fe(II) site of homogentisate dioxygenase | Q27679094 | ||
| Structure of a Dinuclear Iron Cluster-Containing β-Hydroxylase Active in Antibiotic Biosynthesis | Q27679813 | ||
| Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad | Q27729302 | ||
| Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution | Q27730790 | ||
| Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site | Q27741647 | ||
| Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding | Q27741668 | ||
| The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates | Q27748882 | ||
| The role of putidaredoxin and P450 cam in methylene hydroxylation | Q28240049 | ||
| Binding of isotopically labeled substrates, inhibitors, and cyanide by protocatechuate 3,4-dioxygenase | Q28342582 | ||
| Structure and assembly of protocatechuate 3,4-dioxygenase | Q30196085 | ||
| The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. | Q33212392 | ||
| A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis | Q34100542 | ||
| Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme | Q34165579 | ||
| Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: logic, machinery, and mechanisms. | Q34555236 | ||
| A Role of the Putidaredoxin COOH-terminus in P -450 cam (Cytochrome m ) Hydroxylations | Q35128294 | ||
| Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: a new extradiol catecholic dioxygenase | Q36103099 | ||
| Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes | Q36122732 | ||
| Substrate activation for O2 reactions by oxidized metal centers in biology | Q36276760 | ||
| Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b | Q36280329 | ||
| Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases | Q36424496 | ||
| Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant. | Q36441965 | ||
| Simultaneous binding of nitric oxide and isotopically labeled substrates or inhibitors by reduced protocatechuate 3,4-dioxygenase | Q36771074 | ||
| Finding intermediates in the O2 activation pathways of non-heme iron oxygenases. | Q36848901 | ||
| Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. | Q37085698 | ||
| Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases | Q37096285 | ||
| A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases | Q38194935 | ||
| Cytochrome P450cam and its complexes. Mössbauer parameters of the heme iron | Q39075490 | ||
| Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam | Q39077162 | ||
| Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substrates | Q39327808 | ||
| Mössbauer and EPR spectroscopy of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa | Q40037780 | ||
| Protocatechuate 3,4-dioxygenase. Inhibitor studies and mechanistic implications | Q40104742 | ||
| Cytochrome P450 cam: SS- dimer and -SH derivative reactivities | Q40182122 | ||
| Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph. | Q42109246 | ||
| Radical intermediates in monooxygenase reactions of rieske dioxygenases | Q42118290 | ||
| Transition state analogs for protocatechuate 3,4-dioxygenase. Spectroscopic and kinetic studies of the binding reactions of ketonized substrate analogs | Q42246859 | ||
| 17O-water and cyanide ligation by the active site iron of protocatechuate 3,4-dioxygenase. Evidence for displaceable ligands in the native enzyme and in complexes with inhibitors or transition state analogs | Q42246860 | ||
| Intermediate P* from soluble methane monooxygenase contains a diferrous cluster | Q43089844 | ||
| Single turnover chemistry and regulation of O2 activation by the oxygenase component of naphthalene 1,2-dioxygenase | Q43509055 | ||
| Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle | Q43592649 | ||
| Benzoate 1,2-dioxygenase from Pseudomonas putida: single turnover kinetics and regulation of a two-component Rieske dioxygenase | Q44075161 | ||
| Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B. | Q44437408 | ||
| Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme | Q44608174 | ||
| Thiolate ligation of the active site Fe2+ of isopenicillin N synthase derives from substrate rather than endogenous cysteine: spectroscopic studies of site-specific Cys----Ser mutated enzymes | Q44660060 | ||
| Effector proteins from P450(cam) and methane monooxygenase: lessons in tuning nature's powerful reagents | Q44663411 | ||
| Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: single turnover reaction | Q44721367 | ||
| Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase | Q45165821 | ||
| Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates | Q46480177 | ||
| Role of the C-terminal region of the B component of Methylosinus trichosporium OB3b methane monooxygenase in the regulation of oxygen activation | Q46918117 | ||
| Regulation of methane monooxygenase catalysis based on size exclusion and quantum tunneling | Q47350630 | ||
| Mössbauer studies of cytochrome P-450cam | Q48017978 | ||
| EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment | Q50169852 | ||
| Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity. | Q52308271 | ||
| Residues inMethylosinus trichosporiumOB3b Methane Monooxygenase Component B Involved in Molecular Interactions with Reduced- and Oxidized-Hydroxylase Component: A Role for the N-Terminus† | Q57943617 | ||
| Unmasking of Deuterium Kinetic Isotope Effects on the Methane Monooxygenase Compound Q Reaction by Site-Directed Mutagenesis of Component B | Q57943622 | ||
| Kinetics and Activation Thermodynamics of Methane Monooxygenase CompoundQFormation and Reaction with Substrates† | Q57943631 | ||
| An Fe2IVO2 Diamond Core Structure for the Key Intermediate Q of Methane Monooxygenase | Q57943668 | ||
| Large Kinetic Isotope Effects in Methane Oxidation Catalyzed by Methane Monooxygenase: Evidence for C−H Bond Cleavage in a Reaction Cycle Intermediate† | Q57943713 | ||
| Gating Effects of Component B on Oxygen Activation by the Methane Monooxygenase Hydroxylase Component | Q57943718 | ||
| Cytochrome P450cam and its complexes, Mo¨ssbauer parameters of the heme iron | Q57943886 | ||
| Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed reactions. A novel role for protein-protein interactions in an oxygenase mechanism | Q67858553 | ||
| Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction | Q67912113 | ||
| Gentisate 1,2-dioxygenase from pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans | Q68453298 | ||
| Evidence for a mu-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase. Mössbauer and EPR studies | Q69831973 | ||
| [17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases | Q70106014 | ||
| Brevibacterium fuscum protocatechuate 3,4-dioxygenase. Purification, crystallization, and characterization | Q70197659 | ||
| Transient intermediates of the methane monooxygenase catalytic cycle | Q70500721 | ||
| Electron paramagnetic resonance detectable states of cytochrome P-450cam | Q72861271 | ||
| Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters | Q77646438 | ||
| The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450 | Q93648813 | ||
| P433 | issue | 22 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 15141-15153 | |
| P577 | publication date | 2014-04-15 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Life in a sea of oxygen | |
| P478 | volume | 289 |
| Q39078942 | Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants | cites work | P2860 |
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