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.
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Spectroscopic and magnetic studies of wild-type and mutant forms of the Fe(II)- and 2-oxoglutarate-dependent decarboxylase ALKBH4Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analoguesCrystal Structures of Fe2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product IntermediatesSwapping metals in Fe- and Mn-dependent dioxygenases: Evidence for oxygen activation without a change in metal redox stateIntermediate in the O−O Bond Cleavage Reaction of an Extradiol Dioxygenase † , ‡A hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenaseStructural Basis for the Role of Tyrosine 257 of Homoprotocatechuate 2,3-Dioxygenase in Substrate and Oxygen ActivationStructural characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) fromSphingobium chlorophenolicum, a new type of aromatic ring-cleavage enzymeMolecular cloning of the protocatechuate 4,5-dioxygenase genes of Pseudomonas paucimobilisTwo-pronged survival strategy for the major cystic fibrosis pathogen, Pseudomonas aeruginosa, lacking the capacity to degrade nitric oxide during anaerobic respiration.Hydrogen peroxide sensitivity of catechol-2,3-dioxygenase: a cautionary note on use of xylE reporter fusions under aerobic conditionsInsights into the nitric oxide reductase mechanism of flavodiiron proteins from a flavin-free enzymeLife in a sea of oxygen.Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme.Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase.Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: a new extradiol catecholic dioxygenase.Characterization of 2,2',3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium Sphingomonas sp. strain RW1.Spectroscopic studies of the anaerobic enzyme-substrate complex of catechol 1,2-dioxygenaseA Long-Lived Fe(III)-(Hydroperoxo) Intermediate in the Active H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Characterization by Mössbauer, Electron Paramagnetic Resonance, and Density Functional Theory Methods.Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case studyRole of the nonheme Fe(II) center in the biosynthesis of the plant hormone ethylene.Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant.Finding intermediates in the O2 activation pathways of non-heme iron oxygenases.Mechanism of extradiol aromatic ring-cleaving dioxygenases.Enzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies.Versatility of biological non-heme Fe(II) centers in oxygen activation reactions.Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases.Synthetic, spectroscopic, and DFT studies of iron complexes with iminobenzo(semi)quinone ligands: implications for o-aminophenol dioxygenases.A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases.Influence of thiolate ligands on reductive N-O bond activation. Probing the O2(-) binding site of a biomimetic superoxide reductase analogue and examining the proton-dependent reduction of nitrite.Oxygen activation by mononuclear nonheme iron dioxygenases involved in the degradation of aromatics.Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substrates.Characterization of extradiol dioxygenases from a polychlorinated biphenyl-degrading strain that possess higher specificities for chlorinated metabolites.Steady-state kinetics and inhibition of anaerobically purified human homogentisate 1,2-dioxygenase.
P2860
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P2860
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.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年学术文章
@wuu
1986年学术文章
@zh-cn
1986年学术文章
@zh-hans
1986年学术文章
@zh-my
1986年学术文章
@zh-sg
1986年學術文章
@yue
1986年學術文章
@zh
1986年學術文章
@zh-hant
name
Binding of 17O-labeled substra ...... e2+ of extradiol dioxygenases.
@ast
Binding of 17O-labeled substra ...... e2+ of extradiol dioxygenases.
@en
type
label
Binding of 17O-labeled substra ...... e2+ of extradiol dioxygenases.
@ast
Binding of 17O-labeled substra ...... e2+ of extradiol dioxygenases.
@en
prefLabel
Binding of 17O-labeled substra ...... e2+ of extradiol dioxygenases.
@ast
Binding of 17O-labeled substra ...... e2+ of extradiol dioxygenases.
@en
P1476
Binding of 17O-labeled substra ...... e2+ of extradiol dioxygenases.
@en
P2093
D M Arciero
J D Lipscomb
P304
P407
P577
1986-02-01T00:00:00Z