Unsymmetric Dinuclear Rh and RhRh Complexes Supported by Tetraphosphine Ligands and Their Reactivity of Oxidative Protonation and Reductive Dechlorination.

Two linear tetradentate phosphine ligands, -PhPCHP(Ph)CHCHP(Ph)CHPPh ( = CH (-dpmppp), NBn (-dpmppmNBn; Bn = benzyl)) were utilized to synthesize unsymmetrical dinuclear Rh complexes, [RhCl(-dpmppp)(L)] (L = XylNC (), CO ()) and [RhCl(-dpmppmNBn)(L)] (L = XylNC (), CO ()), where electron-deficient Rh → Rh centers with 30 valence electrons are supported by a tetraphosphine in an unusual /- coordination mode. The Rh dimers of - were treated with HCl under air to afford the Rh → Rh dimers with 32 e, [RhCl(-dpmppp)(L)] (L = XylNC (), CO ()) and [RhCl(-dpmppmNBn)(L)] (L = XylNC (), CO ()), via intermediate hydride complexes, [{RhCl(μ-H)RhCl(L)}(-dpmppp)] (L = XylNC (), CO ()) and [{RhCl(μ-H)RhCl(L)}(-dpmppmNBn)] (L = XylNC (), CO ()), and [{Rh(H)Cl(μ-Cl)Rh(L)}-dpmppp)] (L = XylNC (), CO ()) and [{Rh(H)Cl(μ-Cl)Rh(L)}-dpmppmNBn)] (L = XylNC (), CO ()). The hydride intermediates and were monitored under nitrogen by H{P} and P{H} NMR techniques to reveal two reaction pathways depending on the terminal auxiliary ligand L.

Effectiveness of Pharmacist-Physician Collaborative Management for Patients With Idiopathic Pulmonary Fibrosis Receiving Pirfenidone.

Pirfenidone is an anti-fibrotic agent used to treat patients with idiopathic pulmonary fibrosis (IPF). Managing adverse drug events and ensuring compliance with pirfenidone treatment for a prolonged period are important to reduce the rate of disease progression. To maximize the benefits of pirfenidone treatment, we established and evaluated an ambulatory care pharmacy practice, a model of pharmacist-physician collaborative management, for patients receiving pirfenidone.

Endo-beta-mannosidase, a plant enzyme acting on N-glycan: purification, molecular cloning, and characterization.

Endo-beta-mannosidase is a novel endoglycosidase that hydrolyzes the Manbeta1-4GlcNAc linkage in the trimannosyl core structure of N-glycans. This enzyme was partially purified and characterized in a previous report (Sasaki, A., Yamagishi, M.