title: Chloride ligation in inorganic manganese model compounds relevant to photosystem II studied using X-ray absorption spectroscopy.
abstract: Chloride ions are essential for proper function of the photosynthetic oxygen-evolving complex (OEC) of Photosystem II (PS II). Although proposed to be directly ligated to the Mn cluster of the OEC, the specific structural and mechanistic roles of chloride remain unresolved. This study utilizes X-ray absorption spectroscopy (XAS) to characterize the Mn-Cl interaction in inorganic compounds that contain structural motifs similar to those proposed for the OEC. Three sets of model compounds are examined; they possess core structures Mn(IV)(3)O(4)X (X=Cl, F, or OH) that contain a di-micro-oxo and two mono-micro-oxo bridges or Mn(IV)(2)O(2)X (X=Cl, F, OH, OAc) that contain a di-micro-oxo bridge. Each set of compounds is examined for changes in the XAS spectra that are attributable to the replacement of a terminal OH or F ligand, or bridging OAc ligand, by a terminal Cl ligand. The X-ray absorption near edge structure (XANES) shows changes in the spectra on replacement of OH, OAc, or F by Cl ligands that are indicative of the overall charge of the metal atom and are consistent with the electronegativity of the ligand atom. Fourier transforms (FTs) of the extended X-ray absorption fine structure (EXAFS) spectra reveal a feature that is present only in compounds where chloride is directly ligated to Mn. These FT features were simulated using various calculated Mn-X interactions (X=O, N, Cl, F), and the best fits were found when a Mn-Cl interaction at a 2.2-2.3 A bond distance was included. There are very few high-valent Mn halide complexes that have been synthesized, and it is important to make such a comparative study of the XANES and EXAFS spectra because they have the potential for providing information about the possible presence or absence of halide ligation to the Mn cluster in PS II.
authors.affiliation: Melvin Calvin Laboratory, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720-5230, USA.
authors.forename: Shelly A
authors.initials: SA
authors.lastname: Pizarro
authors.forename: Hendrik
authors.initials: H
authors.lastname: Visser
authors.forename: Roehl M
authors.initials: RM
authors.lastname: Cinco
authors.forename: John H
authors.initials: JH
authors.lastname: Robblee
authors.forename: Samudranil
authors.initials: S
authors.lastname: Pal
authors.forename: Sumitra
authors.initials: S
authors.lastname: Mukhopadhyay
authors.forename: Henry J
authors.initials: HJ
authors.lastname: Mok
authors.forename: Kenneth
authors.initials: K
authors.lastname: Sauer
authors.forename: Karl
authors.initials: K
authors.lastname: Wieghardt
authors.forename: William H
authors.initials: WH
authors.lastname: Armstrong
authors.forename: Vittal K
authors.initials: VK
authors.lastname: Yachandra
mesh_terms: D002712:Chlorides / Q000737:chemistry*; D008024:Ligands; D008345:Manganese / Q000737:chemistry*; D008956:Models, Chemical; D045332:Photosystem II Protein Complex / Q000737:chemistry*; D013057:Spectrum Analysis / Q000379:methods; D014965:X-Rays
chemical_list: D002712:Chlorides; D008024:Ligands; D045332:Photosystem II Protein Complex; D008345:Manganese