Pusan National University

About: Pusan National University is a education organization based out in Busan, South Korea. It is known for research contribution in the topics: Catalysis & Population. The organization has 24124 authors who have published 45054 publications receiving 819356 citations. The organization is also known as: Busan National University & Pusan University.

Asymmetric scattering and nonorthogonal mode patterns in optical microspirals

Abstract: Quasibound states in an open system do not in general form an orthogonal and complete basis. It is, however, expected that the nonorthogonality is weak in the case of well-confined states, except close to a so-called exceptional point in parameter space. We present numerical evidence showing that for passive optical microspiral cavities the parameter regime where the nonorthogonality is significant is rather broad. Here we observe almost-degenerate pairs of well-confined modes which are highly nonorthogonal. Using a non-Hermitian model Hamiltonian we demonstrate that this interesting phenomenon is related to the asymmetric scattering between clockwise and counterclockwise propagating waves in the spiral geometry. Numerical simulations of ray dynamics reveal a clear ray-wave correspondence.

Facile synthesis of manganese carbonate quantum dots/Ni(HCO3)2-MnCO3 composites as advanced cathode materials for high energy density asymmetric supercapacitors

Abstract: We have developed a high performance supercapacitor cathode electrode composed of well dispersed MnCO3 quantum dots (QDs, ∼1.2 nm) decorated on nickel hydrogen carbonate–manganese carbonate (Ni(HCO3)2–MnCO3) hedgehog-like shell@needle (MnCO3 QDs/NiH–Mn–CO3) composites directly grown onto a 3D macro-porous nickel foam as a binder-free supercapacitor electrode by a facile and scalable hydrothermal method. The MnCO3 QDs/NiH–Mn–CO3 composite electrode exhibited a remarkable maximum specific capacitance of 2641.3 F g−1 at 3 A g−1 and 1493.3 F g−1 at 15 A g−1. Moreover, the asymmetric supercapacitor with MnCO3 QDs/NiH–Mn–CO3 composites as the positive electrode and graphene as the negative electrode showed an energy density of 58.1 W h kg−1 at a power density of 900 W kg−1 as well as excellent cycling stability with 91.3% retention after 10 000 cycles, which exceeded the energy densities of most previously reported nickel or manganese oxide/hydroxide-based asymmetric supercapacitors. The ultrahigh capacitive performance is attributed to the presence of the high surface area core–shell nanostructure, the well dispersed MnCO3 quantum dots, and the high conductivity of MnCO3 quantum dots as well as the synergetic effect between multiple transition metal ions. The superior supercapacitive performance of the MnCO3 QDs/NiH–Mn–CO3 composites makes them promising cathode materials for high energy density asymmetric supercapacitors.

In vitro activation of pro-phenol-oxidase by two kinds of pro-phenol-oxidase-activating factors isolated from hemolymph of coleopteran, Holotrichia diomphalia larvae

Abstract: Previously, we purified and characterized a pro-phenol-oxidase (pro-PO) of 79 kDa from coleopteran insect, Holotrichia diomphalia larvae [Kwon et al. (1997) Mol. Cells 7, 90−97]. Here, we describe the identification of two pro-PO-activating factors (PPAF), named PPAF-I and PPAF-II, directly involved in the activation of the isolated pro-PO. When pro-PO was incubated with either PPAF-I or PPAF-II, no phenol oxidase activity was observed. However, incubation of pro-PO with both PPAF-I and PPAF-II specifically exhibited phenol oxidase activity. The purified PPAF-I with a molecular mass of 33 kDa on SDS/PAGE had characteristics of a serine protease. It exhibited amidase activity against fluorogenic peptide substrates, tert-butoxycarbonyl-phenylalanyl-seryl-arginyl-4-methylcoumaryl-7-amide being the best among the substrates examined. The activity was completely inhibited by 0.02 mM p-nitrophenyl-p′-guanidinobenzoate HCl and diisopropylflurophosphate. The NH2-terminal sequence of PPAF-I had significant sequence similarity to those of serine proteases. On the other hand, the purified PPAF-II had a molecular mass of 40 kDa on SDS/PAGE and 400 kDa determined by gel filtration, indicating an oligomeric protein. The NH2-terminal sequence of PPAF-II showed no similarity to known proteins. PPAF-II exhibited no amidase activity against the fluorogenic substrates. Reconstitution experiments and immunoblotting analysis using affinity-purified antibody against pro-PO demonstrated that PPAF-I first cleaves the intact pro-PO to an intermediate of 76 kDa with no phenol oxidase activity, and then, PPAF-I converts the intermediate to the active phenol oxidase of 60 kDa in the presence of PPAF-II. These results indicate that the activation of pro-PO system in hemolymph of H. diomphalia larvae is accomplished by at least two activating factors, a serine protease and a protein cofactor.