An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase.
about
Structural Basis for Activation of Class Ib Ribonucleotide ReductaseHigh-resolution crystal structures of the flavoprotein NrdI in oxidized and reduced states--an unusual flavodoxin. Structural biologyEvidence That the β Subunit of Chlamydia trachomatis Ribonucleotide Reductase Is Active with the Manganese Ion of Its Manganese(IV)/Iron(III) Cofactor in Site 1The Dimanganese(II) Site of Bacillus subtilis Class Ib Ribonucleotide ReductaseStructural Basis for Assembly of the Mn IV /Fe III Cofactor in the Class Ic Ribonucleotide Reductase from Chlamydia trachomatisDirect observation of structurally encoded metal discrimination and ether bond formation in a heterodinuclear metalloproteinStreptococcus sanguinis Class Ib Ribonucleotide ReductaseThe origin and evolution of ribonucleotide reductionImplications of the inability of Listeria monocytogenes EGD-e to grow anaerobically due to a deletion in the class III NrdD ribonucleotide reductase for its use as a model laboratory strainStructural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.Ribonucleotide reductase metallocofactor: assembly, maintenance and inhibition.Dark-operative protochlorophyllide oxidoreductase generates substrate radicals by an iron-sulphur cluster in bacteriochlorophyll biosynthesis.Evidence for a Di-μ-oxo Diamond Core in the Mn(IV)/Fe(IV) Activation Intermediate of Ribonucleotide Reductase from Chlamydia trachomatis.Two distinct mechanisms of inactivation of the class Ic ribonucleotide reductase from Chlamydia trachomatis by hydroxyurea: implications for the protein gating of intersubunit electron transfer.Spectroscopic studies of the iron and manganese reconstituted tyrosyl radical in Bacillus cereus ribonucleotide reductase R2 protein.Use of structural phylogenetic networks for classification of the ferritin-like superfamily.Choosing the right metal: case studies of class I ribonucleotide reductasesRapid X-ray photoreduction of dimetal-oxygen cofactors in ribonucleotide reductase.Escherichia coli class Ib ribonucleotide reductase contains a dimanganese(III)-tyrosyl radical cofactor in vivo.Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase.Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins.Superoxide dismutases and superoxide reductases.Bacillus subtilis class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme.Proteome scale comparative modeling for conserved drug and vaccine targets identification in Corynebacterium pseudotuberculosisReaction landscape of a pentadentate N5-ligated Mn(II) complex with O2˙- and H2O2 includes conversion of a peroxomanganese(III) adduct to a bis(μ-oxo)dimanganese(III,IV) species.Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case studyClass I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.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) intermediateGenetic characterization and role in virulence of the ribonucleotide reductases of Streptococcus sanguinisControl of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: diiron or dimanganese?Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear--an intricate bioinorganic workaround to use different metals for the same reaction.Inhibition of chlamydial class Ic ribonucleotide reductase by C-terminal peptides from protein R2.Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteinsRibonucleotide reductases: essential enzymes for bacterial life.NrdH-redoxin protein mediates high enzyme activity in manganese-reconstituted ribonucleotide reductase from Bacillus anthracis.Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.Time-Resolved Investigations of Heterobimetallic Cofactor Assembly in R2lox Reveal Distinct Mn/Fe Intermediates.Divergent mechanisms of iron-containing enzymes for hydrocarbon biosynthesis.Restoration of growth by manganese in a mutant strain of Escherichia coli lacking most known iron and manganese uptake systems.Bacillus anthracis thioredoxin systems, characterization and role as electron donors for ribonucleotide reductase.
P2860
Q27663886-1952DD1D-BA34-4CF2-A76D-A8F8A5D084DCQ27664408-34384D28-ECEC-4B9E-84C2-7E1A7B527BF5Q27676716-D0395126-0173-40FA-B0BB-087EE71C0F96Q27678181-83BF224C-137B-4FBD-BE3C-405B0BDA1DF9Q27679441-4BB683F7-3F82-4E87-9C18-7453192A48CEQ27680193-28D3F198-5EB6-4D61-96CE-18A7AC07AC48Q27681151-4D90C253-B28F-4454-BF89-08D1B391D216Q28649971-82DBFDFC-D9E6-461B-815C-9F554FB1A8D5Q30155593-C4D4ABAB-5C26-484C-B09C-A7FB6C5B440AQ30677281-03635BE4-2BED-4169-BBEE-0A5CD02A0132Q33699869-574C3197-B817-4B0B-8853-3E49BFC1C670Q33807986-BFE9B6FE-CDF4-4F38-9A3F-F802DC50D34CQ33919800-BA7E0FD4-D186-437E-8D26-8F344B56132CQ34092078-54D01D1B-AFC1-4EA0-88D5-F2B90E13ED55Q34202912-73D67F04-0CF2-4A41-AD9E-73A37CC1437FQ34246786-A8CABED2-D757-413A-855D-692E90521132Q34317270-A9F773FC-3F3E-40ED-A2B0-67519B0BBCBBQ34582760-C6B4450A-99B2-47D1-999B-9DC4316A0533Q34790064-698892E9-1B85-4225-9019-80D01B79F17AQ35040660-3D02BB69-5875-4A9F-A0AC-7A1DEEF76D3CQ35040729-F6AADD11-B273-4EB2-BBDE-EB7A2A663C66Q35049047-CD1A9266-4897-4462-8D70-D67AB56C8617Q35087850-3496685E-9BA1-441C-81EE-647E46809B0CQ35540681-416987CE-F736-4166-AC52-92560E0A14A6Q35838133-262B968E-6F83-4F0A-ABDD-471F70F644F5Q36369017-BE52EAF8-E1CC-4E2E-A276-791552BDCF88Q36435630-21C03718-8245-41BE-BF18-0D7F22390920Q37085040-D12800AF-8FB4-4A85-A4B4-40C24B5271E5Q37608585-A8DE3C17-4A29-46BD-95D2-8FD23551D740Q37826997-6F6E6B4F-2C39-405C-B436-CFC50275541BQ37832401-51C8F3F9-2C37-4733-A5A7-20EE73467840Q37850086-BD07F908-6819-4CEF-ABBD-8E4A41FA39FBQ38207520-1FA83BC1-4E6C-47BC-A3A9-045669E2857BQ38210214-3931908E-B771-425E-9C5E-8B5C232B7D75Q38675128-907798D2-B270-4137-A9AE-CC9882C0210CQ38739593-AD143FFB-C684-4182-879C-0426F1AE4FA9Q38749062-6BAAD43A-3B9A-41BB-AD2F-01063735695CQ39048193-3E3FFCB1-46DE-4418-81E7-8D3A333E0BD4Q40361418-44489163-3417-4550-BA6E-80AEAB681115Q41462921-7AAA85B5-FD2D-48A6-A785-D2834C144C6F
P2860
An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին 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
An active dimanganese(III)-tyr ...... s Ib ribonucleotide reductase.
@ast
An active dimanganese(III)-tyr ...... s Ib ribonucleotide reductase.
@en
type
label
An active dimanganese(III)-tyr ...... s Ib ribonucleotide reductase.
@ast
An active dimanganese(III)-tyr ...... s Ib ribonucleotide reductase.
@en
prefLabel
An active dimanganese(III)-tyr ...... s Ib ribonucleotide reductase.
@ast
An active dimanganese(III)-tyr ...... s Ib ribonucleotide reductase.
@en
P2860
P356
P1433
P1476
An active dimanganese(III)-tyr ...... ss Ib ribonucleotide reductase
@en
P2093
Joanne Stubbe
P2860
P304
P356
10.1021/BI902106N
P407
P577
2010-02-01T00:00:00Z