P184
Turning on ribonucleotide reductase by light-initiated amino acid radical generationComplexed Structures of Formylglycinamide Ribonucleotide Amidotransferase from Thermotoga maritima Describe a Novel ATP Binding Protein Superfamily † , ‡N 5 -CAIR Mutase: Role of a CO 2 Binding Site and Substrate Movement in Catalysis † , ‡Formylglycinamide Ribonucleotide Amidotransferase from Thermotoga maritima: Structural Insights into Complex Formation † ‡A Hot Oxidant, 3-NO 2 Y 122 Radical, Unmasks Conformational Gating in Ribonucleotide ReductaseKinetics of Radical Intermediate Formation and Deoxynucleotide Production in 3-Aminotyrosine-Substituted Escherichia coli Ribonucleotide ReductasesNuclear localization of the Saccharomyces cerevisiae ribonucleotide reductase small subunit requires a karyopherin and a WD40 repeat protein.Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers.Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathwaysThe active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo.The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formationA model for the Bacillus subtilis formylglycinamide ribonucleotide amidotransferase multiprotein complex.A chemically competent thiosulfuranyl radical on the Escherichia coli class III ribonucleotide reductaseNanosecond generation of tyrosyl radicals via laser-initiated decaging of oxalate-modified amino acids.Conserved electron donor complex Dre2-Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesisThe class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant.Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer?Photo-ribonucleotide reductase β2 by selective cysteine labeling with a radical phototrigger.Direct observation of a transient tyrosine radical competent for initiating turnover in a photochemical ribonucleotide reductase.Direct Interfacial Y731 Oxidation in α2 by a Photoβ2 Subunit of E. coli Class Ia Ribonucleotide Reductase.Investigation of in vivo diferric tyrosyl radical formation in Saccharomyces cerevisiae Rnr2 protein: requirement of Rnr4 and contribution of Grx3/4 AND Dre2 proteinsRe(bpy)(CO)3CN as a probe of conformational flexibility in a photochemical ribonucleotide reductase.Modulation of Phenol Oxidation in Cofacial Dyads.NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase.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.Mechanism of assembly of the dimanganese-tyrosyl radical cofactor of class Ib ribonucleotide reductase: enzymatic generation of superoxide is required for tyrosine oxidation via a Mn(III)Mn(IV) intermediateFunction of the diiron cluster of Escherichia coli class Ia ribonucleotide reductase in proton-coupled electron transfer.Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase.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.Redox-linked changes to the hydrogen-bonding network of ribonucleotide reductase β2.Use of 3-aminotyrosine to examine the pathway dependence of radical propagation in Escherichia coli ribonucleotide reductase.Kinetics of hydrogen atom abstraction from substrate by an active site thiyl radical in ribonucleotide reductaseImportance of the maintenance pathway in the regulation of the activity of Escherichia coli ribonucleotide reductase.ENDOR spectroscopy and DFT calculations: evidence for the hydrogen-bond network within α2 in the PCET of E. coli ribonucleotide reductase.Charge-Transfer Dynamics at the α/β Subunit Interface of a Photochemical Ribonucleotide Reductase.Hydrogen bond network between amino acid radical intermediates on the proton-coupled electron transfer pathway of E. coli α2 ribonucleotide reductase.
P50
Q24564038-313014AC-AB6D-46CC-8C3B-D3DE31C2B306Q27640435-82BDA442-9EF5-430D-9373-6559C18708D2Q27643814-6C0FAB09-E269-420C-8D13-ECB6A046BD1DQ27651018-8A94C01B-A820-4BE8-BD6E-E9BB31E01287Q27664942-B9AA5020-3792-4101-BEA7-57376D797C93Q27667992-C1902FD8-4941-44E2-8D75-47B0A2C43427Q27933989-CF73DBFA-978E-4FC3-B4BD-576D1F1299EAQ27936412-0E4B591F-E6BA-4A6A-9397-3CDCCAE930E8Q27937332-3BEB526B-1C49-418C-82B6-AA0C84A82E2BQ27937686-5767A734-77BC-4F6D-B18A-41BACCA700DAQ28488897-6E56FA40-2C86-42C0-8BAA-4D69CB38B750Q30163887-3C2CF219-91B3-46A8-A39A-78A7D4BC9D03Q30820473-FACF8209-3CC8-496E-9BD2-737C06E0A719Q30847773-F2C4C2B6-4881-4BAB-8A80-D7D2001882AFQ33674147-A2623853-6417-490F-A456-2F5211B3E063Q34583593-595243E7-F236-42A6-96DB-1378E334AEB8Q35150156-4F2240C6-A247-42A9-8644-39E4D03D8199Q35657634-854D1FE1-FBDC-4DA7-A8AF-4B8F56EE0F8DQ35741467-C7A1170A-DD40-4F40-8C22-6F97C3C695A4Q35822386-C005CA92-07B4-4293-BCFF-2DDE15622D23Q35842180-9032136E-E2A4-4DE0-B231-D6203F08E2CFQ35922912-D2BB105A-67CB-4A9D-A242-36CAA4618838Q36132494-F115B166-15FC-4546-88FD-3E964B0AD089Q36936252-D8566FEB-6F1D-4C6D-92CD-E303FD8A73A9Q37057405-81DC8DD1-9BB4-4FD7-A319-D8149228FC15Q37058245-B9ED7E08-1C6A-4F1A-B86C-028BF9425AC2Q37085040-6AD54E65-5A8E-49A3-A431-8BB19018C4D3Q37407834-CCECC4A2-DB46-4361-B5FE-06A518ABBEA7Q38642680-E1488875-689F-4E74-8849-487941032FFDQ39801996-913FF05E-1B2D-4ED6-AF5B-C534E7AA0377Q40402652-56D54C66-5462-4525-BBC8-C937E2AFEE2AQ41165983-79A9C382-B886-46B4-8D74-7EB8AC0B2AE2Q41522967-3BB1FE9E-B0F9-4946-BC9A-51342D02467EQ41549682-F1154F74-5C0E-414D-A219-93BCB92B6541Q41848953-CF1C7FDC-4D86-4452-A4A0-459C6A4CF419Q42072501-E17DD861-C06E-43C6-847E-719ED0E36831Q42158590-3C0D38EA-37CB-41E1-BCD8-6BD789535F5CQ42238479-42BC7058-50EE-426C-97A0-B15BEAF0BAC9Q42530068-C898B181-C794-4F87-9E32-C88F0C05509CQ42554367-F9AAFC6B-AF87-4986-9A18-377136666E58
P50
description
Ameerika Ühendriikide keemik
@et
American chemist
@en
Amerikaans scheikundige
@nl
Usana kemiisto
@io
amerikanische Biochemikerin
@de
amerikansk kemiker
@da
amerikansk kemist
@sv
amerikansk kjemikar
@nn
amerikansk kjemiker
@nb
bioquimico estadounidense
@es
name
JoAnne Stubbe
@ast
JoAnne Stubbe
@ca
JoAnne Stubbe
@cy
JoAnne Stubbe
@da
JoAnne Stubbe
@de
JoAnne Stubbe
@en
JoAnne Stubbe
@en-ca
JoAnne Stubbe
@en-gb
JoAnne Stubbe
@es
JoAnne Stubbe
@fr
type
label
JoAnne Stubbe
@ast
JoAnne Stubbe
@ca
JoAnne Stubbe
@cy
JoAnne Stubbe
@da
JoAnne Stubbe
@de
JoAnne Stubbe
@en
JoAnne Stubbe
@en-ca
JoAnne Stubbe
@en-gb
JoAnne Stubbe
@es
JoAnne Stubbe
@fr
prefLabel
JoAnne Stubbe
@ast
JoAnne Stubbe
@ca
JoAnne Stubbe
@cy
JoAnne Stubbe
@da
JoAnne Stubbe
@de
JoAnne Stubbe
@en
JoAnne Stubbe
@en-ca
JoAnne Stubbe
@en-gb
JoAnne Stubbe
@es
JoAnne Stubbe
@fr
P106
P166
P463
P166
P185
P19
P21
P2381
P31
P496
0000-0001-8076-4489
P5380
P569
1946-06-11T00:00:00Z