Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme.
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Ring-cleaving dioxygenases with a cupin foldA hyperactive cobalt-substituted extradiol-cleaving catechol dioxygenaseStructural Basis for the Role of Tyrosine 257 of Homoprotocatechuate 2,3-Dioxygenase in Substrate and Oxygen ActivationHuman 3-hydroxyanthranilate 3,4-dioxygenase () dynamics and reaction, a multilevel computational study.Characterization of a paramagnetic mononuclear nonheme iron-superoxo complex.Life in a sea of oxygen.The photochemistry of [Fe(III)N3(cyclam-ac)]PF6 at 266 nm.Evidence that the fosfomycin-producing epoxidase, HppE, is a non-heme-iron peroxidaseCharacterization of an O2 adduct of an active cobalt-substituted extradiol-cleaving catechol dioxygenaseCrystal structures of alkylperoxo and anhydride intermediates in an intradiol ring-cleaving dioxygenase.Nitrosyl hydride (HNO) replaces dioxygen in nitroxygenase activity of manganese quercetin dioxygenaseO(2)-evolving chlorite dismutase as a tool for studying O(2)-utilizing enzymes.Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200A 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.Axial and equatorial ligand effects on biomimetic cysteine dioxygenase model complexes3,4-Dihydroxyphenylacetate 2,3-dioxygenase from Pseudomonas aeruginosa: An Fe(II)-containing enzyme with fast turnover.Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case studySubstrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant.Spectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin.Substrate Promotes Productive Gas Binding in the α-Ketoglutarate-Dependent Oxygenase FIH.Crystallographic and spectroscopic characterization and reactivities of a mononuclear non-haem iron(III)-superoxo complex.Enzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies.Spectroscopic Evidence for the Two C-H-Cleaving Intermediates of Aspergillus nidulans Isopenicillin N Synthase.Oxygen-18 Kinetic Isotope Effects of Nonheme Iron Enzymes HEPD and MPnS Support Iron(III) Superoxide as the Hydrogen Abstraction SpeciesNovel Approaches for the Accumulation of Oxygenated Intermediates to Multi-Millimolar Concentrations.Quantitative Interpretation of Multifrequency Multimode EPR Spectra of Metal Containing Proteins, Enzymes, and Biomimetic Complexes.Synthetic, spectroscopic, and DFT studies of iron complexes with iminobenzo(semi)quinone ligands: implications for o-aminophenol dioxygenases.Dioxygen reactivity of biomimetic Fe(II) complexes with noninnocent catecholate, o-aminophenolate, and o-phenylenediamine ligands.A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases.Electronic structure analysis of the oxygen-activation mechanism by Fe(II)- and α-ketoglutarate (αKG)-dependent dioxygenases.Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center.Catalytic Mechanism of Salicylate Dioxygenase: QM/MM Simulations Reveal the Origin of Unexpected Regioselectivity of the Ring Cleavage.Mono- and binuclear non-heme iron chemistry from a theoretical perspective.Go it alone: four-electron oxidations by mononuclear non-heme iron enzymes.Oxygen activation by mononuclear Mn, Co, and Ni centers in biology and synthetic complexes.O-H Activation by an Unexpected Ferryl Intermediate during Catalysis by 2-Hydroxyethylphosphonate Dioxygenase.Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.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.NO binding to Mn-substituted homoprotocatechuate 2,3-dioxygenase: relationship to O₂ reactivity.
P2860
Q24605922-5C283C6B-512B-4804-8528-0BE804C261B5Q27666296-CC6B78DC-BBF2-47EA-8627-ACD7FBE49CEAQ27674540-B41E2344-78C1-4160-903D-2C92C649AFF9Q30370777-F8FA7A2A-8BD2-4694-9CAF-9371E94D6D45Q34045550-C97A0FFA-CE2D-4645-BAA4-5548980DACD2Q34075835-4AE9F530-4C60-4CC8-A379-BC61A2CCB3C3Q34148748-2716A110-0232-4C5D-B846-B7ADAA3B8F46Q34163009-29E5E41A-CC1F-47CD-8448-E12120960F10Q34241151-A3C1DDF7-B868-4B4F-83D5-9AC72772E9CBQ34985604-3FFF8BCF-5419-4F92-A704-5247B67D8BF4Q35571299-94B5C16E-44CF-4B00-8CE8-EEAE4252D08FQ35814819-0D743B99-7D53-4A6A-B3A6-CD73BB0C9DEEQ36021557-B74FA403-5677-4606-AFAC-E1536AF3FFF4Q36240394-CA092D17-661F-4E45-9C11-AEF1FB2FC302Q36266480-62A800F0-BE52-44A7-900E-FA86549D3FA9Q36269705-258F1434-A86C-4B3F-A90F-449860B8A832Q36369017-CDB601CD-F9FB-4C34-A123-DB89577CD5C7Q36441965-F8B0FE10-58D2-4029-8D4D-8D5D5A2EC955Q36571170-D450FD1D-7923-4E88-9812-8BDA6E6C6B7FQ36691958-09D18494-C8AF-4B80-923B-5E938260515CQ36817622-35A96CAB-CB5D-4176-A7CC-25DB9B663FB6Q37047077-3805633E-513B-4241-955F-312E97025900Q37116091-02ED9E73-1762-4342-9ECA-C2CD07E1CCE0Q37146242-110CB6A7-2065-43A4-9C7E-18105E505BF4Q37407850-02FCEBFE-F8CE-4902-AE33-B3557BBF7C08Q37618394-568F8C03-A256-4280-A593-94C4E06F0911Q37662376-9E13E1D0-BCF7-43F8-9365-16FFA1D42444Q37721709-F53F3D5D-160C-4133-B9B2-29EEDB323C1DQ38194935-0BA4FE44-E9EE-47AD-9285-07B45BCF40C9Q38287167-E63671AB-F08B-4C8C-8C3E-D56632183FECQ38792167-F4E44C48-6817-4E70-80EC-969D63387DECQ38818871-FE7B4AC7-8B3B-4682-905A-F74E7B12A633Q38845297-521BFA0A-45B3-4100-A66A-7EC2199E077FQ38991287-C9B5A835-0F41-4D39-94BA-F541B55903F7Q39010642-991FD192-C9C2-4DAB-9F77-C574A51EA4CBQ39018157-B62600D7-8347-496A-BC95-A67A7AA444FCQ39078942-1ED91921-75B3-4C51-8F99-49BD1FAB1BB7Q39085404-55C74F66-8830-4BCF-ADCC-5BD446CC67F4Q39327808-DCF8F122-CD0C-4679-A484-0E0C907AA8ACQ41904863-2D688158-2A0F-465B-8ACF-44ABC42B6A88
P2860
Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@ast
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@en
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@nl
type
label
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@ast
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@en
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@nl
prefLabel
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@ast
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@en
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@nl
P2093
P2860
P356
P1476
Trapping and spectroscopic cha ...... uclear iron-containing enzyme.
@en
P2093
Eckard Münck
Emile L Bominaar
John D Lipscomb
Joshua A Hayden
Michael M Mbughuni
Michael P Hendrich
Mrinmoy Chakrabarti
P2860
P304
16788-16793
P356
10.1073/PNAS.1010015107
P407
P577
2010-09-13T00:00:00Z