Advances and challenges in shale oil development: A critical review

    Different from the conventional oil reservoirs, the primary storage space of shale is micro/nano pore networks. Moreover, the multiscale and multi-minerals characteristics of shale also attract increasing attentions from researchers. In this work, the advances and challenges in the development of shale oil are summarized from following aspects: phase behavior, flow mechanisms, reservoir numerical simulation and production optimization. The phase behavior of fluids confined in shale nanopores are discussed on the basis of theoretical calculations, experiments, and molecular simulations. The fluid transport mechanisms through shale matrix are analyzed in terms of molecular dynamics, pore scale simulations, and experimental studies. The methods employed in fracture propagation simulation and production optimization of shale oil are also introduced. Clarifying the problems of current research and the need for future studies are conducive to promoting the scientific and effective development of shale oil resources.Cited as: Feng, Q., Xu, S., Xing, X., Zhang, W., Wang, S. Advances and challenges in shale oil development: A critical review. Advances in Geo-Energy Research, 2020, 4(4), 406-418, doi: 10.46690/ager.2020.04.0

High-Throughput Screening of Transition Metal Single-Atom Catalysts for Nitrogen Reduction Reaction

The discovery of metals as catalytic centers for nitrogen reduction reactions has stimulated great enthusiasm for single-atom catalysts. However, the poor activity and low selectivity of available SACs are far away from the industrial requirement. Through the high throughout first principles calculations, the doping engineering can effectively regulate the NRR performance of b-Sb monolayer. Especially, the origin of activated N2 is revealed from the perspective of the electronic structure of the active center. Among the 24 transition metal dopants, Re@Sb and Tc@Sb showed the best NRR catalytic performance with a low limiting potential. The Re@Sb and Tc@Sb also could significantly inhibit HER and achieve a high theoretical Faradaic efficiency of 100%. Our findings not only accelerate discovery of catalysts for ammonia synthesis but also contribute to further elucidate the structure-performance correlations

OSBP-Related Protein 8 (ORP8) Regulates Plasma and Liver Tissue Lipid Levels and Interacts with the Nucleoporin Nup62

Peer reviewe

Structural and mechanistic insights into the biosynthesis of CDP-archaeol in membranes

The divergence of archaea, bacteria and eukaryotes was a fundamental step in evolution. One marker of this event is a major difference in membrane lipid chemistry between these kingdoms. Whereas the membranes of bacteria and eukaryotes primarily consist of straight fatty acids ester-bonded to glycerol-3-phosphate, archaeal phospholipids consist of isoprenoid chains ether-bonded to glycerol-1-phosphate. Notably, the mechanisms underlying the biosynthesis of these lipids remain elusive. Here, we report the structure of the CDP-archaeol synthase (CarS) of Aeropyrum pernix (ApCarS) in the CTP- and Mg(2+)-bound state at a resolution of 2.4 Å. The enzyme comprises a transmembrane domain with five helices and cytoplasmic loops that together form a large charged cavity providing a binding site for CTP. Identification of the binding location of CTP and Mg(2+) enabled modeling of the specific lipophilic substrate-binding site, which was supported by site-directed mutagenesis, substrate-binding affinity analyses, and enzyme assays. We propose that archaeol binds within two hydrophobic membrane-embedded grooves formed by the flexible transmembrane helix 5 (TM5), together with TM1 and TM4. Collectively, structural comparisons and analyses, combined with functional studies, not only elucidated the mechanism governing the biosynthesis of phospholipids with ether-bonded isoprenoid chains by CTP transferase, but also provided insights into the evolution of this enzyme superfamily from archaea to bacteria and eukaryotes.Cell Research advance online publication 29 September 2017; doi:10.1038/cr.2017.122

Structural and Functional Insights into an Archaeal Lipid Synthase

The UbiA superfamily of intramembrane prenyltransferases catalyzes an isoprenyl transfer reaction in the biosynthesis of lipophilic compounds involved in cellular physiological processes. Digeranylgeranylglyceryl phosphate (DGGGP) synthase (DGGGPase) generates unique membrane core lipids for the formation of the ether bond between the glycerol moiety and the alkyl chains in archaea and has been confirmed to be a member of the UbiA superfamily. Here, the crystal structure is reported to exhibit nine transmembrane helices along with a large lateral opening covered by a cytosolic cap domain and a unique substrate-binding central cavity. Notably, the lipid-bound states of this enzyme demonstrate that the putative substrate-binding pocket is occupied by the lipidic molecules used for crystallization, indicating the binding mode of hydrophobic substrates. Collectively, these structural and functional studies provide not only an understanding of lipid biosynthesis by substrate-specific lipid-modifying enzymes but also insights into the mechanisms of lipid membrane remodeling and adaptation