Dioxygen activation at non-heme diiron centers: characterization of intermediates in a mutant form of toluene/o-xylene monooxygenase hydroxylase.
about
X-ray Structure of a Hydroxylase−Regulatory Protein Complex from a Hydrocarbon-Oxidizing Multicomponent Monooxygenase, Pseudomonas sp. OX1 Phenol Hydroxylase † , ‡Dioxygen Activation at Non-Heme Diiron Centers: Oxidation of a Proximal Residue in the I100W Variant of Toluene/ o -Xylene Monooxygenase Hydroxylase †Tracking a defined route for O2 migration in a dioxygen-activating diiron enzymeCrystal structure of a substrate complex of myo-inositol oxygenase, a di-iron oxygenase with a key role in inositol metabolismmyo-Inositol oxygenase: a radical new pathway for O(2) and C-H activation at a nonheme diiron clusterCharacterization of two distinct adducts in the reaction of a nonheme diiron(II) complex with O2.Synthesis, Characterization, and Oxygenation Studies of Carboxylate-Bridged Diiron(II) Complexes with Aromatic Substrates Tethered to Pyridine Ligands and the Formation of a Unique Trinuclear Complex.Multiple roles of component proteins in bacterial multicomponent monooxygenases: phenol hydroxylase and toluene/o-xylene monooxygenase from Pseudomonas sp. OX1.Mechanistic studies of reactions of peroxodiiron(III) intermediates in T201 variants of toluene/o-xylene monooxygenase hydroxylaseX-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior.Protonation of a peroxodiiron(III) complex and conversion to a diiron(III/IV) intermediate: implications for proton-assisted O-O bond cleavage in nonheme diiron enzymes.Iron complexes of dendrimer-appended carboxylates for activating dioxygen and oxidizing hydrocarbons.Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins.Factors affecting the carboxylate shift upon formation of nonheme diiron-O2 adducts.Human deoxyhypusine hydroxylase, an enzyme involved in regulating cell growth, activates O2 with a nonheme diiron centerCharacterization of a peroxodiiron(III) intermediate in the T201S variant of toluene/o-xylene monooxygenase hydroxylase from Pseudomonas sp. OX1Modeling the syn disposition of nitrogen donors in non-heme diiron enzymes. Synthesis, characterization, and hydrogen peroxide reactivity of diiron(III) complexes with the syn N-donor ligand H2BPG2DEV.Novel Approaches for the Accumulation of Oxygenated Intermediates to Multi-Millimolar Concentrations.Circular dichroism, magnetic circular dichroism, and variable temperature variable field magnetic circular dichroism studies of biferrous and mixed-valent myo-inositol oxygenase: insights into substrate activation of O2 reactivity.Cyanobacterial aldehyde deformylase oxygenation of aldehydes yields n-1 aldehydes and alcohols in addition to alkanes.Microbial enzymes for aromatic compound hydroxylation.Molecular-Level Insight into the Differential Oxidase and Oxygenase Reactivities of de Novo Due Ferri Proteins.Spectroscopic evidence for the presence of a high-valent Fe(IV) species in the ferroxidase reaction of an archaeal ferritin.Characterization of the arene-oxidizing intermediate in ToMOH as a diiron(III) species.X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5aOxygen reactivity of the biferrous site in the de novo designed four helix bundle peptide DFsc: nature of the "intermediate" and reaction mechanism.The prediction of Fe Mössbauer parameters by the density functional theory: a benchmark study.Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.
P2860
Q27640833-E9DED87B-1CB8-4E45-A2E8-9CC65A4443DCQ27649158-FBD1D377-059B-4CC1-A44C-8B0CD0BE35DCQ27671902-4D8C7739-01BE-4B6E-90AB-903C2926E650Q28266269-F55BDA49-D459-49A9-9A10-030F6BB5FFE8Q28307759-9E2B4C50-E9DD-4E76-94E5-06C90D3EDF89Q33757560-FE3AC4C6-D67F-4608-81DD-0BEF4C57DF7AQ33768083-FD54178F-1401-429D-82EE-9247C09E90F6Q34687284-D31C602A-8D0D-4462-B119-A9A9EE7EEC2BQ35048876-3607D90B-1550-4D43-A5B4-14BF49A759BDQ35568292-F308637F-63E8-4C0F-9566-DCF5B08B828BQ36291375-15293AAF-6A5E-4293-B9B4-9E5BBED0CC2EQ36676776-C466E807-3CDA-463A-A53F-A2B29AD48344Q36872282-F9FE5D27-B5D1-4DF1-80D4-29FC3AEE1BE2Q36918565-47AD4327-55DC-45D0-8B7B-14B71A0DA680Q37329690-4659EADF-84DE-4294-BA14-4EBF768109B5Q37351308-304BDBDD-6069-46EF-A182-68F37D54C510Q37380042-2794F754-8129-4CF9-97C7-7E6F9CF7108BQ37407850-6F065E98-7CC5-43DC-9ADA-3371D3101D72Q37439406-8F61CBF6-98DD-4A44-8559-A18CBA7AEAF2Q37520342-88086461-AD0B-4A7E-9348-898B3696BAA1Q37869399-3750325F-B802-4860-8148-F038C357DF1BQ40582071-FC3B4B7E-6935-4738-876D-4468126E9553Q41077091-E82A58C5-75CD-4EF2-84A5-793C9F2C1CB5Q41280148-7F4018EC-EE1E-4D72-9DD0-A00B9E3BDF14Q41581853-5C980201-8759-457D-A2FB-626FF7EB69EAQ41825766-6360A16E-AE7A-48E8-8347-93B0B45CD9EAQ42000164-9CDBEF27-A968-4EAC-BB2E-C55AB7DEC6FFQ48105963-701E0FCB-B6E9-4228-A1D4-5090E58BAD09
P2860
Dioxygen activation at non-heme diiron centers: characterization of intermediates in a mutant form of toluene/o-xylene monooxygenase hydroxylase.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Dioxygen activation at non-hem ...... ene monooxygenase hydroxylase.
@en
type
label
Dioxygen activation at non-hem ...... ene monooxygenase hydroxylase.
@en
prefLabel
Dioxygen activation at non-hem ...... ene monooxygenase hydroxylase.
@en
P2093
P2860
P356
P1476
Dioxygen activation at non-hem ...... ene monooxygenase hydroxylase.
@en
P2093
Boi Hanh Huynh
Ricardo García-Serres
Sunil Naik
P2860
P304
P356
10.1021/JA062762L
P407
P577
2006-06-01T00:00:00Z