Mono-, di-, tri-, and tetra-substituted fluorotyrosines: new probes for enzymes that use tyrosyl radicals in catalysis.
about
Molecular eyes: proteins that transform light into biological informationMechanisms for control of biological electron transfer reactionsSite-Specific Incorporation of 3-Nitrotyrosine as a Probe of p K a Perturbation of Redox-Active Tyrosines in Ribonucleotide ReductaseA Hot Oxidant, 3-NO 2 Y 122 Radical, Unmasks Conformational Gating in Ribonucleotide ReductaseA genetically encoded 19F NMR probe for tyrosine phosphorylationSynthesis of 3,5-difluorotyrosine-containing peptides: application in substrate profiling of protein tyrosine phosphatases.Using unnatural amino acids to probe the energetics of oxyanion hole hydrogen bonds in the ketosteroid isomerase active site.Proton-coupled electron flow in protein redox machinesProton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology.Proton-coupled electron transfer in biology: results from synergistic studies in natural and model systems.Chemistry of personalized solar energy.Proton coupled electron transfer and redox active tyrosines in Photosystem IIDeciphering radical transport in the large subunit of class I ribonucleotide reductaseDirect observation of a transient tyrosine radical competent for initiating turnover in a photochemical ribonucleotide reductase.Comparative PCET study of a donor-acceptor pair linked by ionized and nonionized asymmetric hydrogen-bonded interfaces.Direct Interfacial Y731 Oxidation in α2 by a Photoβ2 Subunit of E. coli Class Ia Ribonucleotide Reductase.Mechanism of the AppABLUF Photocycle Probed by Site-Specific Incorporation of Fluorotyrosine Residues: Effect of the Y21 pKa on the Forward and Reverse Ground-State ReactionsRe(bpy)(CO)3CN as a probe of conformational flexibility in a photochemical ribonucleotide reductase.Significant Improvement of Oxidase Activity through the Genetic Incorporation of a Redox-active Unnatural Amino Acid.Defining the role of tyrosine and rational tuning of oxidase activity by genetic incorporation of unnatural tyrosine analogs.Replacement of Y730 and Y731 in the alpha2 subunit of Escherichia coli ribonucleotide reductase with 3-aminotyrosine using an evolved suppressor tRNA/tRNA-synthetase pair.Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an ExamplePhotochemical Generation of a Tryptophan Radical within the Subunit Interface of Ribonucleotide Reductase.Rapid kinetics of dehalogenation promoted by iodotyrosine deiodinase from human thyroid.Probing the coupling between proton and electron transfer in photosystem II core complexes containing a 3-fluorotyrosine.Distance-independent charge recombination kinetics in cytochrome c-cytochrome c peroxidase complexes: compensating changes in the electronic coupling and reorganization energiesBLUF domain function does not require a metastable radical intermediate state.Photoinduced proton-coupled electron transfers in biorelevant phenolic systems.Fluorinated amino acids: compatibility with native protein structures and effects on protein-protein interactions.Redox modulation of flavin and tyrosine determines photoinduced proton-coupled electron transfer and photoactivation of BLUF photoreceptors.Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase.Organic fluorine as a polypeptide building element: in vivo expression of fluorinated peptides, proteins and proteomes.Visible and ultraviolet spectroscopy of gas phase protein ions.Equilibration of tyrosyl radicals (Y356•, Y731•, Y730•) in the radical propagation pathway of the Escherichia coli class Ia ribonucleotide reductase.Use of 2,3,5-F(3)Y-β2 and 3-NH(2)Y-α2 to study proton-coupled electron transfer in Escherichia coli ribonucleotide reductase.Reverse Electron Transfer Completes the Catalytic Cycle in a 2,3,5-Trifluorotyrosine-Substituted Ribonucleotide Reductase.A >200 meV Uphill Thermodynamic Landscape for Radical Transport in Escherichia coli Ribonucleotide Reductase Determined Using Fluorotyrosine-Substituted Enzymes.Formal reduction potential of 3,5-difluorotyrosine in a structured protein: insight into multistep radical transfer.Kinetics of hydrogen atom abstraction from substrate by an active site thiyl radical in ribonucleotide reductaseCharge-Transfer Dynamics at the α/β Subunit Interface of a Photochemical Ribonucleotide Reductase.
P2860
Q26853118-30F4A426-3719-4BB6-90B6-957A1C423856Q26866918-FB24F963-E4FF-4990-BB3A-4F8DDB106204Q27662095-E8DB25AF-8065-4E88-9A3E-77911B0C2347Q27664942-D77CB7BD-14A1-47C1-AB44-2D68FEBBF6C2Q27684095-879C72EB-FA63-4A45-8879-B9382814C89BQ33370184-4EB4C61D-8B48-4FB3-8340-26C8AE16BFF1Q33716390-5746250C-F200-48B6-A954-AB8874619F3EQ34423826-4F3DA6A8-F084-4409-8658-830E86780A8FQ34551745-3D298BDB-5DEB-4705-AA5D-7760276EAB96Q34974036-16523AC8-E5CD-43F0-AFE8-C5D0A5297906Q35004698-D6D45C7C-7CE7-476C-ACDA-8544B76B959FQ35189808-85075DCD-C3BE-4B38-9D68-04D097A19C9BQ35712576-6A34BB62-EFBF-4B18-9CC4-E946AEA4A52AQ35741467-1ACE3DE2-7EA4-4319-B680-B6D1BED90590Q35753637-024AEF61-CD0D-440C-8D2B-624481B7FFE6Q35822386-4D5E6466-83A0-4212-BF7E-57845D1114A9Q35879115-C17E5249-B3B6-4860-A19A-26EA11F7C8DBQ35922912-F816E720-9164-4AE6-8505-642D5CDF025EQ36093517-450FE0BD-8B31-43FF-AF4E-1CC3FF8BD661Q36364982-001974DA-D234-4F5F-87C9-257655760C5AQ36461216-678D6F56-4E62-438A-81AA-03EC223EE55DQ37057405-413457B3-46CE-4D62-81F0-A2B004C18A42Q37058245-C30C4E36-0B22-464F-B958-A4B2E3A88349Q37078503-8555DE63-F6EF-4844-87D9-AB238931FCD6Q37193895-ED19972E-A27F-48EA-B045-DD3987C70524Q37257161-D7DFB72B-95F2-4384-8503-22E63619FB5DQ37731540-FB049094-D723-4A90-85FD-9B866907CFBEQ37927136-7DF9F3D1-E67F-4373-A507-3F297B93CCE1Q37963228-9B7DA1A8-B8E2-459C-B2B0-885C2127D1FEQ38323197-426F4BA8-08CC-48AD-A90D-9375A3AFBDCDQ38642680-92628CF4-BFF3-472E-94B1-281A09143DE8Q39569652-B9B08B0C-B812-46F7-AAB3-4BC5887E2E90Q39721582-E863C449-AA67-4E2A-A7E6-7B803C0A3537Q39754152-BB23E643-18F3-4877-8F34-6DBF3FA6F6B0Q39801996-C065771D-9345-4A2A-9328-2A7C8BAB7411Q40402652-ED60573A-FC04-4A91-8D98-C03F8524058DQ41165983-2335E6D2-D473-4089-ACD2-393F00AF34EDQ41522967-5BF47535-D9C8-44D4-B3F9-ADD8F5BBBA64Q42072501-448261BF-2DEA-46ED-886A-477365BC3F99Q42530068-EC2AE1E2-633A-4D4E-81C0-64193F9F8D21
P2860
Mono-, di-, tri-, and tetra-substituted fluorotyrosines: new probes for enzymes that use tyrosyl radicals in catalysis.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Mono-, di-, tri-, and tetra-su ...... tyrosyl radicals in catalysis.
@en
Mono-, di-, tri-, and tetra-su ...... tyrosyl radicals in catalysis.
@nl
type
label
Mono-, di-, tri-, and tetra-su ...... tyrosyl radicals in catalysis.
@en
Mono-, di-, tri-, and tetra-su ...... tyrosyl radicals in catalysis.
@nl
prefLabel
Mono-, di-, tri-, and tetra-su ...... tyrosyl radicals in catalysis.
@en
Mono-, di-, tri-, and tetra-su ...... tyrosyl radicals in catalysis.
@nl
P2093
P356
P1476
Mono-, di-, tri-, and tetra-su ...... tyrosyl radicals in catalysis.
@en
P2093
Daniel G Nocera
Joanne Stubbe
Mohammad R Seyedsayamdost
Steven Y Reece
P304
P356
10.1021/JA055926R
P407
P577
2006-02-01T00:00:00Z