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A CO-derived iron dicarbyne that releases olefin upon hydrogenation.

ABSTRACT: An iron diphosphineborane platform that was previously reported to facilitate a high degree of N2 functionalization is herein shown to effect reductive CO coupling. Disilylation of an iron dicarbonyl precursor furnishes a structurally unprecedented iron dicarbyne complex. Several complexes related to this process are also characterized which allows for a comparative analysis of their respective Fe-B and Fe-C bonding. Facile hydrogenation of the iron dicarbyne at ambient temperature and 1 atm H2 results in release of a CO-derived olefin.

SUBMITTER: Suess DL

PROVIDER: S-EPMC3794666 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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A CO-derived iron dicarbyne that releases olefin upon hydrogenation.

Suess Daniel L M DL Peters Jonas C JC

Journal of the American Chemical Society 20130819 34

An iron diphosphineborane platform that was previously reported to facilitate a high degree of N2 functionalization is herein shown to effect reductive CO coupling. Disilylation of an iron dicarbonyl precursor furnishes a structurally unprecedented iron dicarbyne complex. Several complexes related to this process are also characterized which allows for a comparative analysis of their respective Fe-B and Fe-C bonding. Facile hydrogenation of the iron dicarbyne at ambient temperature and 1 atm H2 ...[more]

PMID: 23931747

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Project description:The human astrovirus (HAstV) is a non-enveloped, single-stranded RNA virus that is a common cause of gastroenteritis. Most non-enveloped viruses use membrane disruption to deliver the viral genome into a host cell after virus uptake. The virus-host factors that allow for HAstV cell entry are currently unknown but thought to be associated with the host-protease-mediated viral maturation. Using in vitro liposome disruption analysis, we identified a trypsin-dependent lipid disruption activity in the capsid protein of HAstV serotype 8. This function was further localized to the P1 domain of the viral capsid core, which was both necessary and sufficient for membrane disruption. Site-directed mutagenesis identified a cluster of four trypsin cleavage sites necessary to retain the lipid disruption activity, which is likely attributed to a short stretch of sequence ending at arginine 313 based on mass spectrometry of liposome-associated peptides. The membrane disruption activity was conserved across several other HAstVs, including the emerging VA2 strain, and effective against a wide range of lipid identities. This work provides key functional insight into the protease maturation process essential to HAstV infectivity and presents a method to investigate membrane penetration by non-enveloped viruses in vitro. IMPORTANCE Human astroviruses (HAstVs) are an understudied family of viruses that cause mild gastroenteritis but have recent cases associated with a more severe neural pathogenesis. Many important elements of the HAstV life cycle are not well understood, and further elucidating them can help understand the various forms of HAstV pathogenesis. In this study, we utilized an in vitro liposome-based assay to describe and characterize a previously unreported lipid disruption activity. This activity is dependent on the protease cleavage of key sites in HAstV capsid core and can be controlled by site-directed mutagenesis. Our group observed this activity in multiple strains of HAstV and in multiple lipid conditions, indicating this may be a conserved activity across the AstV family. The discovery of this function provides insight into HAstV cellular entry, pathogenesis, and a possible target for future therapeutics.

Dataset Information

A CO-derived iron dicarbyne that releases olefin upon hydrogenation.

Publications

A CO-derived iron dicarbyne that releases olefin upon hydrogenation.

Similar Datasets

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