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Issue 2, 2014
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EXAFS simulation refinement based on broken-symmetry DFT geometries for the Mn(IV)–Fe(III) center of class I RNR from Chlamydia trachomatis

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Abstract

Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides into deoxyribonucleotides necessary for DNA biosynthesis. Unlike the conventional class Ia RNRs which use a diiron cofactor in their subunit R2, the active site of the RNR-R2 from Chlamydia trachomatis (Ct) contains a Mn/Fe cofactor. The detailed structure of the Mn/Fe core has yet to be established. In this paper we evaluate six different structural models of the Ct RNR active site in the Mn(IV)/Fe(III) state by using Mössbauer parameter calculations and simulations of Mn/Fe extended X-ray absorption fine structure (EXAFS) spectroscopy, and we identify a structure similar to a previously proposed DFT-optimized model that shows quantitative agreement with both EXAFS and Mössbauer spectroscopic data.

Graphical abstract: EXAFS simulation refinement based on broken-symmetry DFT geometries for the Mn(iv)–Fe(iii) center of class I RNR from Chlamydia trachomatis

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Publication details

The article was received on 13 Jun 2013, accepted on 07 Oct 2013 and first published on 16 Oct 2013


Article type: Paper
DOI: 10.1039/C3DT51563J
Citation: Dalton Trans., 2014,43, 576-583
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    EXAFS simulation refinement based on broken-symmetry DFT geometries for the Mn(IV)–Fe(III) center of class I RNR from Chlamydia trachomatis

    S. Luber, S. Leung, C. Herrmann, W. H. Du, L. Noodleman and V. S. Batista, Dalton Trans., 2014, 43, 576
    DOI: 10.1039/C3DT51563J

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