title: EXAFS simulation refinement based on broken-symmetry DFT geometries for the Mn(IV)-Fe(III) center of class I RNR from Chlamydia trachomatis.
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.
authors.affiliation: Department of Chemistry, Yale University, P.O. Box 208107, New Haven, CT 06520, USA. victor.batista@yale.edu.
authors.forename: Sandra
authors.initials: S
authors.lastname: Luber
authors.forename: Sophie
authors.initials: S
authors.lastname: Leung
authors.forename: Carmen
authors.initials: C
authors.lastname: Herrmann
authors.forename: Wenge Han
authors.initials: WH
authors.lastname: Du
authors.forename: Louis
authors.initials: L
authors.lastname: Noodleman
authors.forename: Victor S
authors.initials: VS
authors.lastname: Batista
mesh_terms: D020134:Catalytic Domain; D002692:Chlamydia trachomatis / Q000201:enzymology*; D007501:Iron; D008345:Manganese; D011789:Quantum Theory; D012264:Ribonucleotide Reductases / Q000737:chemistry*; D056928:X-Ray Absorption Spectroscopy
chemical_list: D008345:Manganese; D007501:Iron; D012264:Ribonucleotide Reductases