The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state.
about
Evidence That the β Subunit of Chlamydia trachomatis Ribonucleotide Reductase Is Active with the Manganese Ion of Its Manganese(IV)/Iron(III) Cofactor in Site 1Structural Basis for Assembly of the Mn IV /Fe III Cofactor in the Class Ic Ribonucleotide Reductase from Chlamydia trachomatisEvidence 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.Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase.Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins.O(2)-evolving chlorite dismutase as a tool for studying O(2)-utilizing enzymes.Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.A manganese(IV)/iron(IV) intermediate in assembly of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase.Branched activation- and catalysis-specific pathways for electron relay to the manganese/iron cofactor in ribonucleotide reductase from Chlamydia trachomatis.Formation and function of the Manganese(IV)/Iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductaseNovel Approaches for the Accumulation of Oxygenated Intermediates to Multi-Millimolar Concentrations.Geometric and electronic structure of the Mn(IV)Fe(III) cofactor in class Ic ribonucleotide reductase: correlation to the class Ia binuclear non-heme iron enzyme.Structural analysis of the Mn(IV)/Fe(III) cofactor of Chlamydia trachomatis ribonucleotide reductase by extended X-ray absorption fine structure spectroscopy and density functional theory calculations.Radical-translocation intermediates and hurdling of pathway defects in "super-oxidized" (Mn(IV)/Fe(IV)) Chlamydia trachomatis ribonucleotide reductase.Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear--an intricate bioinorganic workaround to use different metals for the same reaction.Geometrical properties of the manganese(iv)/iron(iii) cofactor of Chlamydia trachomatis ribonucleotide reductase unveiled by simulations of XAS spectra.Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase from Chlamydia trachomatis.EXAFS simulation refinement based on broken-symmetry DFT geometries for the Mn(IV)-Fe(III) center of class I RNR from Chlamydia trachomatis.Density functional theory analysis of structure, energetics, and spectroscopy for the Mn-Fe active site of Chlamydia trachomatis ribonucleotide reductase in four oxidation states.Redox intermediates of the Mn-Fe Site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: an X-ray absorption and EPR study.Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteinsElectron hopping through proteins.Mössbauer properties of the diferric cluster and the differential iron(II)-binding affinity of the iron sites in protein R2 of class Ia Escherichia coli ribonucleotide reductase: a DFT/electrostatics study.
P2860
Q27676716-24742AF1-84D4-4192-ADD8-FE5A8FE652A3Q27679441-7FE1EB5A-EAB8-4291-B176-BABF3A6DBB7AQ33919800-A988FB91-BC72-4155-91E9-9DA32986CC62Q34092078-239EBDCA-3A7C-4AA4-83F1-B80ABB64A151Q34202912-B5E25489-9850-49C7-82BC-D44AAB7D6122Q34752841-F6E745BC-BE3E-4B79-90EC-E01C781957CBQ35040729-A2B84AA6-3680-4249-A438-C33C1E11AAD0Q35814819-60C37447-0869-46C2-BF4B-6203B9A0B135Q36435630-77E51D14-1AD7-4B6F-9E88-9BBA4F91131BQ36851963-9847A48F-0617-45BB-8B46-0B846DBB7232Q37189692-BFF33F04-7DF9-4C1C-954F-777B7B344564Q37218969-E700DA19-44AB-49AA-A192-FE8D7D82FDF3Q37407850-84F2F4C2-E2FB-40B0-BC43-9779DB559E01Q37439394-2A5D4EE3-E6A1-485D-8E16-5F2702984565Q37474552-923D37A4-4621-46EC-8D2B-E92D3DF3DF66Q37597145-4F8179D7-AC27-4E63-AC85-471EAF641F2CQ37832401-F856D11A-BC7D-448D-A631-FD6E6D2BF0F8Q37834620-A2B910A9-565A-44AF-81AF-7B3C592CEA59Q37840226-0AE93EA0-6913-4542-A717-00260224AB78Q37845681-99A6AC7F-35C8-4E1E-AC45-A8236CA2728FQ37852767-E515F1BD-9DC2-4BB7-B5CE-C2BA1482D771Q37855926-CFA6C2E1-840D-400D-AB5A-5FC6AF0BEA0AQ38207520-108FF089-0CDE-46BA-BDCF-3AE41BE02FF0Q42099315-A2810292-02B6-44FB-BF74-C0607642E1ECQ43137381-43916A57-45D2-4E26-AB01-3C60E3223FC0
P2860
The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 27 May 2007
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The active form of Chlamydia t ...... contains a heterodinuclear Mn
@nl
The active form of Chlamydia t ...... uster with S = 1 ground state.
@en
type
label
The active form of Chlamydia t ...... contains a heterodinuclear Mn
@nl
The active form of Chlamydia t ...... uster with S = 1 ground state.
@en
prefLabel
The active form of Chlamydia t ...... contains a heterodinuclear Mn
@nl
The active form of Chlamydia t ...... uster with S = 1 ground state.
@en
P2860
P356
P1476
The active form of Chlamydia t ...... uster with S = 1 ground state.
@en
P2093
J Martin Bollinger
P2860
P304
P356
10.1021/JA072528A
P407
P577
2007-05-27T00:00:00Z