Mesostructural study on graphenic-based carbon prepared from coconut shells by heat treatment and liquid exfoliation.

In this study, the effect of heating temperature on the structure of graphenic-based carbon (GC) has been successfully investigated. A series of GC materials was prepared from coconut shells by a green synthesis method. The process includes heating at four temperatures (T = 400, 600, 800 and 1000 °C) followed by an exfoliation process assisted by hydrochloric acid (HCl). These materials were characterized by wide- and small-angle x-ray scattering (WAXS and SAXS), Fourier-transform infrared spectroscopy (FTIR), x-ray photoemission spectroscopy (XPS) and transmission electron microscopy (TEM). The WAXS analysis shows Braggs peaks corresponding to the reduced graphene oxide (rGO)-like phase. Investigations by FTIR and XPS methods show the presence of carbon-oxygen functional groups such as C=C (carbon with sp 2 hybridization), C-C (carbon with sp 3 hybridization), and C=O bonds. The sp 2 bonds form a 2-dimensional (2D) network in hexagonal lattice, while carbon with sp 3 bonds tends to form a 3-dimensional (3D) tetrahedral structure. The BET analysis revealed meso- and micro-pore structures in GC. Heating process reduces the specific surface area and increases pore size of GC. Moreover, increasing the heating temperature induces a decrease in radius of gyration (R g) and an increase in the formation of 2D structures in GC. The fitting results of SAXS profiles, proved by TEM and XPS, yielded the structure of GC containing the mixture of 2D and 3D structures. Thus, it is suggested that the GC has a mesostructure.

Solution Structure and Conformational Dynamics of a Doublet Acyl Carrier Protein from Prodigiosin Biosynthesis.

The acyl carrier protein (ACP) is an indispensable component of both fatty acid and polyketide synthases and is primarily responsible for delivering acyl intermediates to enzymatic partners. At present, increasing numbers of multidomain ACPs have been discovered with roles in molecular recognition of trans-acting enzymatic partners as well as increasing metabolic flux. Further structural information is required to provide insight into their function, yet to date, the only high-resolution structure of this class to be determined is that of the doublet ACP (two continuous ACP domains) from mupirocin synthase. Here we report the solution nuclear magnetic resonance (NMR) structure of the doublet ACP domains from PigH (PigH ACP1-ACP2), which is an enzyme that catalyzes the formation of the bipyrrolic intermediate of prodigiosin, a potent anticancer compound with a variety of biological activities. The PigH ACP1-ACP2 structure shows each ACP domain consists of three conserved helices connected by a linker that is partially restricted by interactions with the ACP1 domain. Analysis of the holo (4'-phosphopantetheine, 4'-PP) form of PigH ACP1-ACP2 by NMR revealed conformational exchange found predominantly in the ACP2 domain reflecting the inherent plasticity of this ACP. Furthermore, ensemble models obtained from SAXS data reveal two distinct conformers, bent and extended, of both apo (unmodified) and holo PigH ACP1-ACP2 mediated by the central linker. The bent conformer appears to be a result of linker-ACP1 interactions detected by NMR and might be important for intradomain communication during the biosynthesis. These results provide new insights into the behavior of the interdomain linker of multiple ACP domains that may modulate protein-protein interactions. This is likely to become an increasingly important consideration for metabolic engineering in prodigiosin and other related biosynthetic pathways.