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Triamidoamine thorium-arsenic complexes with parent arsenide, arsinidiide and arsenido structural motifs.

ABSTRACT: Despite a major expansion of uranium-ligand multiple bond chemistry in recent years, analogous complexes involving other actinides (An) remain scarce. For thorium, under ambient conditions only a few multiple bonds to carbon, nitrogen, phosphorus and chalcogenides are reported, and none to arsenic are known; indeed only two complexes with thorium-arsenic single bonds have been structurally authenticated, reflecting the challenges of stabilizing polar linkages at the large thorium ion. Here, we report thorium parent-arsenide (ThAsH₂), -arsinidiides (ThAs(H)K and ThAs(H)Th) and arsenido (ThAsTh) linkages stabilized by a bulky triamidoamine ligand. The ThAs(H)K and ThAsTh linkages exhibit polarized-covalent thorium-arsenic multiple bonding interactions, hitherto restricted to cryogenic matrix isolation experiments, and the AnAs(H)An and AnAsAn linkages reported here have no precedent in f-block chemistry. 7s, 6d and 5f orbital contributions to the Th-As bonds are suggested by quantum chemical calculations, and their compositions unexpectedly appear to be tensioned differently compared to phosphorus congeners.

SUBMITTER: Wildman EP

PROVIDER: S-EPMC5347141 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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Triamidoamine thorium-arsenic complexes with parent arsenide, arsinidiide and arsenido structural motifs.

Wildman Elizabeth P EP Balázs Gábor G Wooles Ashley J AJ Scheer Manfred M Liddle Stephen T ST

Nature communications 20170309

Despite a major expansion of uranium-ligand multiple bond chemistry in recent years, analogous complexes involving other actinides (An) remain scarce. For thorium, under ambient conditions only a few multiple bonds to carbon, nitrogen, phosphorus and chalcogenides are reported, and none to arsenic are known; indeed only two complexes with thorium-arsenic single bonds have been structurally authenticated, reflecting the challenges of stabilizing polar linkages at the large thorium ion. Here, we r ...[more]

PMID: 28276437

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Project description:BACKGROUND: A lot of high-throughput studies produce protein-protein interaction networks (PPINs) with many errors and missing information. Even for genome-wide approaches, there is often a low overlap between PPINs produced by different studies. Second-level neighbors separated by two protein-protein interactions (PPIs) were previously used for predicting protein function and finding complexes in high-error PPINs. We retrieve second level neighbors in PPINs, and complement these with structural domain-domain interactions (SDDIs) representing binding evidence on proteins, forming PPI-SDDI-PPI triangles. RESULTS: We find low overlap between PPINs, SDDIs and known complexes, all well below 10%. We evaluate the overlap of PPI-SDDI-PPI triangles with known complexes from Munich Information center for Protein Sequences (MIPS). PPI-SDDI-PPI triangles have ~20 times higher overlap with MIPS complexes than using second-level neighbors in PPINs without SDDIs. The biological interpretation for triangles is that a SDDI causes two proteins to be observed with common interaction partners in high-throughput experiments. The relatively few SDDIs overlapping with PPINs are part of highly connected SDDI components, and are more likely to be detected in experimental studies. We demonstrate the utility of PPI-SDDI-PPI triangles by reconstructing myosin-actin processes in the nucleus, cytoplasm, and cytoskeleton, which were not obvious in the original PPIN. Using other complementary datatypes in place of SDDIs to form triangles, such as PubMed co-occurrences or threading information, results in a similar ability to find protein complexes. CONCLUSION: Given high-error PPINs with missing information, triangles of mixed datatypes are a promising direction for finding protein complexes. Integrating PPINs with SDDIs improves finding complexes. Structural SDDIs partially explain the high functional similarity of second-level neighbors in PPINs. We estimate that relatively little structural information would be sufficient for finding complexes involving most of the proteins and interactions in a typical PPIN.

Dataset Information

Triamidoamine thorium-arsenic complexes with parent arsenide, arsinidiide and arsenido structural motifs.

Publications

Triamidoamine thorium-arsenic complexes with parent arsenide, arsinidiide and arsenido structural motifs.

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