Selective Synthesis and Crystal Structure of [10]Cycloparaphenylene

[10]Cycloparaphenylene ([10]CPP) was selectively synthesized in four steps in 13% overall yield from commercially available 4,4′-diiodobiphenyl by using mono-I–Sn exchange, Sn–Pt transmetalation, I–Pd exchange, and subsequent oxidative coupling reactions. The single-crystal X-ray structure of [10]CPP is described

Selective Synthesis and Crystal Structure of [10]Cycloparaphenylene

[10]Cycloparaphenylene ([10]CPP) was selectively synthesized in four steps in 13% overall yield from commercially available 4,4′-diiodobiphenyl by using mono-I–Sn exchange, Sn–Pt transmetalation, I–Pd exchange, and subsequent oxidative coupling reactions. The single-crystal X-ray structure of [10]CPP is described

Importance of the Conserved Lysine 83 Residue of <i>Zea mays</i> Cytochrome <i>b</i>₅₆₁ for Ascorbate-Specific Transmembrane Electron Transfer As Revealed by Site-Directed Mutagenesis Studies

Cytochromes b561, a novel class of transmembrane electron transport proteins residing in a large variety of eukaryotic cells, have a number of common structural features including six hydrophobic transmembrane α-helices and two heme ligation sites. We found that recombinant Zea mays cytochrome b561 obtained by a heterologous expression system using yeast Pichia pastoris cells could utilize the ascorbate/mondehydroascorbate radical as a physiological electron donor/acceptor. We found further that a concerted proton/electron transfer mechanism might be operative in Z. mays cytochrome b561 as well upon the electron acceptance from ascorbate to the cytosolic heme center. The well-conserved Lys83 residue in a cytosolic loop was found to have a very important role(s) for the binding of ascorbate and the succeeding electron transfer via electrostatic interactions based on the analyses of three site-specific mutants, K83A, K83E, and K83D. Further, unusual behavior of the K83A mutant in pulse radiolysis experiments indicated that Lys83 might also be responsible for the intramolecular electron transfer to the intravesicular heme. On the other hand, pulse radiolysis experiments on two site-specific mutants, S118A and W122A, for the well-conserved residues in the putative monodehydroascorbate radical binding site showed that their electron transfer activities to the monodehydroascorbate radical were very similar to those of the wild-type protein, indicating that Ser118 and Trp122 do not have major roles for the redox events on the intravesicular side

Adsorption-Induced Intramolecular Dipole: Correlating Molecular Conformation and Interface Electronic Structure

The interfaces formed between pentacene (PEN) and perfluoropentacene (PFP) molecules and Cu(111) were studied using photoelectron spectroscopy, X-ray standing wave (XSW), and scanning tunneling microscopy measurements, in conjunction with theoretical modeling. The average carbon bonding distances for PEN and PFP differ strongly, that is, 2.34 Å for PEN versus 2.98 Å for PFP. An adsorption-induced nonplanar conformation of PFP is suggested by XSW (F atoms 0.1 Å above the carbon plane), which causes an intramolecular dipole of ∼0.5 D. These observations explain why the hole injection barriers at both molecule/metal interfaces are comparable (1.10 eV for PEN and 1.35 eV for PFP) whereas the molecular ionization energies differ significantly (5.00 eV for PEN and 5.85 eV for PFP). Our results show that the hypothesis of charge injection barrier tuning at organic/metal interfaces by adjusting the ionization energy of molecules is not always readily applicable

Supplementary Table 2 from MEK Inhibitor for Gastric Cancer with <i>MEK1</i> Gene Mutations

Supplementary Table 2: Patient characteristics.</p

Supplementary Table 1 from MEK Inhibitor for Gastric Cancer with <i>MEK1</i> Gene Mutations

Supplementary Table 1: Primers for sequencing and mutagenesis.</p

Supplementary Table Legends from MEK Inhibitor for Gastric Cancer with <i>MEK1</i> Gene Mutations

The captions of Supplementary Tables 1 and 2.</p