Structural Analysis of the Mn(IV)/Fe(III) Cofactor of Chiamydia trachomatis Ribonucleotide Reductase by Extended X-ray Absorption Fine Structure Spectroscopy and Density Functional Theory Calculations.
The class Ic ribonucleotide reductase from Chiamydia trachomatis (Ct) uses a stable Mn(lV)/Fe(lll) cofactor to initiate nucleotide reduction by a free-radical mechanism. Extended X-ray absorption fine structure (EXAFS) spectroscopy and density functional theory (OFT) calculations are used to postula...
| Publicado en: | Journal of the American Chemical Society Vol. 130; no. 45; pp. 15022 - 15028 |
|---|---|
| Autores principales: | , , , , , |
| Formato: | Artículo |
| Publicado: |
American Chemical Society
11/12/2008
|
| Materias: | |
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=35398450&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 35398450 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 11/12/2008 vid: 130 iid: 45 pid: 997 pub: American Chemical Society artinfo: ui: 35398450 10.1021/ja804365e ppf: 15022 ppct: 6 formats: tig: atl: Structural Analysis of the Mn(IV)/Fe(III) Cofactor of Chiamydia trachomatis Ribonucleotide Reductase by Extended X-ray Absorption Fine Structure Spectroscopy and Density Functional Theory Calculations. aug: au: Younker, Jarod M. Krest, Courtney M. Jiang, Wel Krebs, Carsten Bollinger Jr., J. Martin Green, Michael T. affil: Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802 Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802 su: Structural analysis (Science) Manganese Iron Deoxyribonucleotides Extended X-ray absorption fine structure Density functionals Proton transfer reactions Metal ions sug: subj: Structural analysis (Science) Manganese Iron Deoxyribonucleotides Extended X-ray absorption fine structure Density functionals Proton transfer reactions Metal ions ab: The class Ic ribonucleotide reductase from Chiamydia trachomatis (Ct) uses a stable Mn(lV)/Fe(lll) cofactor to initiate nucleotide reduction by a free-radical mechanism. Extended X-ray absorption fine structure (EXAFS) spectroscopy and density functional theory (OFT) calculations are used to postulate a structure for this cofactor. Fe and Mn K-edge EXAFS data yield an intermetallic distance of ∼2.92 A. The Mn data also suggest the presence of a short 1.74 Å Mn-O bond. These metrics are compared to the results of DFT calculations on 12 cofactor models derived from the crystal structure of the inactive Fe2(lll/Ill) form of the protein. Models are differentiated by the protonation states of their bridging and terminal OH[subx] ligands as well as the location of the Mn(IV) ion (site 1 or 2). The models that agree best with experimental observation feature a μ-1,3-carboxylate bridge (E120), terminal solvent (H[sub2]O/OH) to site 1, one μ-O bridge, and one μ-OH bridge. The site-placement of the metal ions cannot be discerned from the available data. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2008 holdings: @attributes: islocal: N |
|---|