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Issue 14, 2017
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Geometrical properties of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase unveiled by simulations of XAS spectra

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Abstract

Using simulations of Mn/Fe K-edge X-ray absorption spectroscopy (XAS), combined with DFT-optimized structural models and direct comparisons with available experimental data, we determine geometrical and electronic properties of the Mn–Fe active site of Chlamydia trachomatis (Ct) of ribonucleotide reductase (RNR). In the post-edge XAS energy range, we use extended X-ray absorption fine structure (EXAFS) data, to acquire absorber–scatterer geometrical information around each absorber metal center. For this task, we apply a protocol that evaluates Debye–Waller factors in scattering paths instead of scattering shells to fit the experimental EXAFS. The model of the manganese(IV)/iron(III) cofactor that best fit Mn and Fe K-edge EXAFS experimental data is a structure with Mn at metal site 1 (proximal to Phe-127), a μ-oxo/μ-hydroxo/μ-1,3-carboxylato core, and a terminal hydroxo ligand, i.e. OH–Mn1(IV)–(μ-O)(μ-OH)-Fe2(III).

Graphical abstract: Geometrical properties of the manganese(iv)/iron(iii) cofactor of Chlamydia trachomatis ribonucleotide reductase unveiled by simulations of XAS spectra

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Publication details

The article was received on 09 Oct 2016, accepted on 06 Mar 2017 and first published on 15 Mar 2017


Article type: Paper
DOI: 10.1039/C6DT03893J
Citation: Dalton Trans., 2017,46, 4724-4736
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    Geometrical properties of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase unveiled by simulations of XAS spectra

    E. M. Sproviero, Dalton Trans., 2017, 46, 4724
    DOI: 10.1039/C6DT03893J

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