Jack Cheng

Bio: Jack Cheng is an academic researcher from China Medical University (Taiwan). The author has contributed to research in topics: Imidazole & Medicine. The author has an hindex of 12, co-authored 39 publications receiving 454 citations. Previous affiliations of Jack Cheng include National Tsing Hua University.

Structural studies and photochromism of mercury(II)-iodo complexes of (arylazo)imidazoles.

Abstract: Neat reaction between HgI2 and 1-methyl-2-(phenylazo)imidazole (Pai-Me) under microwave irradiation has isolated a novel compound whose structure shows intercalated HgI2 in the layers of Pai-Me. They exist independently in interpenetrated arrays. In a solution phase study, the same reaction has synthesized an iodo-bridged azoimidazole−Hg(II) complex, [Hg(RaaiR‘)(μ-I)(I)]2 (RaaiR‘ = 1-alkyl-2-(arylazo)imidazole). The structures have been characterized by X-ray diffraction studies. Chloro-bridged Hg(II) complexes of azoimidazoles, [Hg(RaaiR‘)(μ-Cl)(Cl)]2, are also known. These complexes upon irradiation with UV light show trans-to-cis isomerization. The reverse transformation, cis-to-trans isomerization, is very slow with visible light irradiation. Quantum yields (φt→c) of trans-to-cis isomerization are calculated, and the free ligand shows higher φ than their Hg(II) complexes. The cis-to-trans isomerization is a thermally induced process. The activation energy (Ea) of cis-to-trans isomerization is calculat...

LRIG1 modulates aggressiveness of head and neck cancers by regulating EGFR-MAPK-SPHK1 signaling and extracellular matrix remodeling.

Abstract: EGFR overexpression and chromosome 3p deletion are two frequent events in head and neck cancers. We previously mapped the smallest region of recurrent copy-number loss at 3p12.2-p14.1. LRIG1, a negative regulator of EGFR, was found at 3p14, and its copy-number loss correlated with poor clinical outcome. Inducible expression of LRIG1 in head and neck cancer TW01 cells, a line with low LRIG1 levels, suppressed cell proliferation in vitro and tumor growth in vivo. Gene expression profiling, quantitative RT-PCR, chromatin immunoprecipitation, and western blot analysis demonstrated that LRIG1 modulated extracellular matrix (ECM) remodeling and EGFR-MAPK-SPHK1 transduction pathway by suppressing expression of EGFR ligands/activators, MMPs and SPHK1. In addition, LRIG1 induction triggered cell morphology changes and integrin inactivation, which coupled with reduced SNAI2 expression. By contrast, knockdown of endogenous LRIG1 in TW06 cells, a line with normal LRIG1 levels, significantly enhanced cell proliferation, migration and invasiveness. Such tumor-promoting effects could be abolished by specific MAPK or SPHK1 inhibitors. Our data suggest LRIG1 as a tumor suppressor for head and neck cancers; LRIG1 downregulation in cancer cells enhances EGFR-MAPK-SPHK1 signaling and ECM remodeling activity, leading to malignant phenotypes of head and neck cancers.

Proton-Coupled Electron Transfer

Abstract: ▪ Abstract Proton-coupled electron transfer (PCET) is an important mechanism for charge transfer in a wide variety of systems including biology- and materials-oriented venues. We review several are...

Signaling Receptors for TGF-β Family Members

Abstract: Transforming growth factor beta (TGF-beta) family members signal via heterotetrameric complexes of type I and type II dual specificity kinase receptors. The activation and stability of the receptor ...

Mechanisms of water oxidation from the blue dimer to photosystem II

Abstract: The blue dimer, cis, cis-[(bpy)2(H2O)Ru(III)ORu(III)(H2O)(bpy)2](4+), is the first designed, well-defined molecule known to function as a catalyst for water oxidation. It meets the stoichiometric requirements for water oxidation, 2H2O --> -4e(-), -4H(+) O-O, by utilizing proton-coupled electron-transfer (PCET) reactions in which both electrons and protons are transferred. This avoids charge buildup, allowing for the accumulation of multiple oxidative equivalents at the Ru-O-Ru core. PCET and pathways involving coupled electron-proton transfer (EPT) are also used to avoid high-energy intermediates. Application of density functional theory calculations to molecular and electronic structure supports the proposal of strong electronic coupling across the micro-oxo bridge. The results of this analysis provide explanations for important details of the descriptive chemistry. Stepwise e(-)/H(+) loss leads to the higher oxidation states [(bpy)2(O)Ru(V)ORu(IV)(O)(bpy)2] (3+) (Ru(V)ORu(IV)) and [(bpy)2(O)Ru(V)ORu(V)(O)(bpy)2](4+) (Ru(V)ORu(V)). Both oxidize water, Ru(V)ORu(IV) stoichiometrically and Ru(V)ORu(V) catalytically. In strongly acidic solutions (HNO3, HClO4, and HSO3CF3) with excess Ce(IV), the catalytic mechanism involves O---O coupling following oxidation to Ru(V)ORu(V), which does not build up as a detectable intermediate. Direct evidence has been found for intervention of a peroxidic intermediate. Oxidation of water by Ru(V)ORu(IV) is far slower. It plays a role late in the catalytic cycle when Ce(IV) is depleted and is one origin of anated intermediates such as [(bpy)2(HO)Ru(IV)ORu(IV)(NO3)(bpy)2](4+), which are deleterious in tying up active components in the catalytic cycle. These intermediates slowly return to [(bpy)2(H2O)Ru(IV)ORu(III)(OH2)(bpy)2](5+) with anion release followed by water oxidation. The results of a recent analysis of water oxidation in the oxygen-evolving complex (OEC) of photosystem II reveal similarities in the mechanism with the blue dimer and significant differences. The OEC resides in the thylakoid membrane in the chloroplasts of green plants, and careful attention is paid in the structure to PCET, EPT, and long-range proton transfer by sequential local proton transfers. The active site for water oxidation is a CaMn 4 cluster, which includes an appended Mn site, Mn(4), where O---O coupling is thought to occur. Photochemical electron transfer results in oxidation of tyrosine Y Z to Y Z (.), which is approximately 7 A from Mn(4). It subsequently oxidizes the OEC through the stepwise stages of the Kok cycle. O---O coupling appears to occur through an initial peroxidic intermediate formed by redox nucleophilic attack of coordinated OH(-) in Ca-OH(-) on Mn (IV)=O.