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Structural and physical properties diversity of new CaCu5-type related europium platinum borides.

ABSTRACT: Three novel europium platinum borides have been synthesized by arc melting of constituent elements and subsequent annealing. They were characterized by X-ray powder and single-crystal diffraction: EuPt4B, CeCo4B type, P6/mmm, a = 0.56167(2) nm, c = 0.74399(3) nm; Eu3Pt7B2, Ca3Al7Cu2 type as an ordered variant of PuNi3, R3m, a = 0.55477(2) nm, c = 2.2896(1) nm; and Eu5Pt18B(6-x), a new unique structure type, Fmmm, a = 0.55813(3) nm, b = 0.95476(5) nm, c = 3.51578(2) nm. These compounds belong to the CaCu5 family of structures, revealing a stacking sequence of CaCu5-type slabs with different structural units: CaCu5 and CeCo3B2 type in EuPt4B; CeCo3B2 and Laves MgCu2 type in Eu3Pt7B2; and CaCu5-, CeCo3B2-, and site-exchange ThCr2Si2-type slabs in Eu5Pt18B(6-x). The striking motif in the Eu5Pt18B(6-x) structure is the boron-centered Pt tetrahedron [BPt4], which build chains running along the a axis and plays a decisive role in the structure arrangement by linking the terminal fragments of repeating blocks of fused Eu polyhedra. Physical properties of two compounds, EuPt4B and Eu3Pt7B2, were studied. Both compounds were found to order magnetically at 36 and 57 K, respectively. For EuPt4B a mixed-valence state of the Eu atom was confirmed via magnetic and specific heat measurements. Moreover, the Sommerfeld value of the specific heat of Eu3Pt7B2 was found to be extraordinarily large, on the order of 0.2 J/mol?K(2).

SUBMITTER: Salamakha L

PROVIDER: S-EPMC3627515 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Structural and physical properties diversity of new CaCu5-type related europium platinum borides.

Salamakha Leonid L Bauer Ernst E Hilscher Gerfried G Michor Herwig H Sologub Oksana O Rogl Peter P Giester Gerald G

Inorganic chemistry 20130329 8

Three novel europium platinum borides have been synthesized by arc melting of constituent elements and subsequent annealing. They were characterized by X-ray powder and single-crystal diffraction: EuPt4B, CeCo4B type, P6/mmm, a = 0.56167(2) nm, c = 0.74399(3) nm; Eu3Pt7B2, Ca3Al7Cu2 type as an ordered variant of PuNi3, R3m, a = 0.55477(2) nm, c = 2.2896(1) nm; and Eu5Pt18B(6-x), a new unique structure type, Fmmm, a = 0.55813(3) nm, b = 0.95476(5) nm, c = 3.51578(2) nm. These compounds belong to ...[more]

PMID: 23540751

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Project description:The widespread bacterial second messenger cyclic diguanylate (c-di-GMP) regulates a variety of processes, including protein secretion, motility, cell development, and biofilm formation. c-di-GMP-dependent responses are often mediated by its binding to the cytoplasmic receptors that contain the PilZ domain. Here, we present comparative structural and sequence analysis of various PilZ-related domains and describe three principal types of them: (i) the canonical PilZ domain, whose structure includes a six-stranded beta-barrel and a C-terminal alpha helix, (ii) an atypical PilZ domain that contains two extra alpha helices and forms stable tetramers, and (iii) divergent PilZ-related domains, which include the eponymous PilZ protein and PilZN (YcgR_N) and PilZNR (YcgR_2) domains. We refine the second c-di-GMP binding motif of PilZ as [D/N]hSXXG and show that the hydrophobic residue h of this motif interacts with a cluster of conserved hydrophobic residues, helping maintain the PilZ domain fold. We describe several novel PilZN-type domains that are fused to the canonical PilZ domains in specific taxa, such as spirochetes, actinobacteria, aquificae, cellulose-degrading clostridia, and deltaproteobacteria. We propose that the evolution of the three major groups of PilZ domains included (i) fusion of pilZ with other genes, which produced Alg44, cellulose synthase, and other multidomain proteins; (ii) insertion of an ∼200-bp fragment, which resulted in the formation of tetramer-forming PilZ proteins; and (iii) tandem duplication of pilZ genes, which led to the formation of PilZ dimers and YcgR-like proteins.IMPORTANCE c-di-GMP is a ubiquitous bacterial second messenger that regulates motility, biofilm formation, and virulence of many bacterial pathogens. The PilZ domain is a widespread c-di-GMP receptor that binds c-di-GMP through its RXXXR and [D/N]hSXXG motifs; some PilZ domains lack these motifs and are unable to bind c-di-GMP. We used structural and sequence analysis to assess the diversity of PilZ-related domains and define their common features. We show that the hydrophobic residue h in the second position of the second motif is highly conserved; it may serve as a readout for c-di-GMP binding. We describe three principal classes of PilZ-related domains, canonical, tetramer-forming, and divergent PilZ domains, and propose the evolutionary pathways that led to the emergence of these PilZ types.

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Structural and physical properties diversity of new CaCu5-type related europium platinum borides.

Publications

Structural and physical properties diversity of new CaCu5-type related europium platinum borides.

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