Intramolecular Light-Driven Accumulation of Reduction Equivalents by Proton-Coupled Electron Transfer

The photochemistry of a molecular pentad composed of a central anthraquinone (AQ) acceptor flanked by two Ru(bpy)32+ photosensitizers and two peripheral triarylamine (TAA) donors was investigated by transient IR and UV–vis spectroscopies in the presence of 0.2 M p-toluenesulfonic acid (TsOH) in deaerated acetonitrile. In ∼15% of all excited pentad molecules, AQ is converted to its hydroquinone form (AQH2) via reversible intramolecular electron transfer from the two TAA units (τ = 65 ps), followed by intermolecular proton transfer from TsOH (τ ≈ 3 ns for the first step). Although the light-driven accumulation of reduction equivalents occurs through a sequence of electron and proton transfer steps, the resulting photoproduct decays via concerted PCET (τ = 4.7 μs) with an H/D kinetic isotope effect of 1.4 ± 0.2. Moreover, the reoxidation of AQH2 seems to take place via a double electron transfer step involving both TAA+ units rather than sequential single electron transfer events. Thus, the overall charge-recombination reaction seems to involve a concerted proton-coupled two-electron oxidation of AQH2. The comparison of experimental data obtained in neat acetonitrile with data from acidic solutions suggests that the inverted driving-force effect can play a crucial role for obtaining long-lived photoproducts resulting from multiphoton, multielectron processes. Our pentad provides the first example of light-driven accumulation of reduction equivalents stabilized by PCET in artificial molecular systems without sacrificial reagents. Our study provides fundamental insight into how light-driven multielectron redox chemistry, for example the reduction of CO2 or the oxidation of H2O, can potentially be performed without sacrificial reagents

Sentence Comprehension and Repetition in Conduction Aphasia: Results of Parallel Testing

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Cardiac risk factors and risk scores vs cardiac computed tomography angiography: a prospective cohort study for triage of ED patients with acute chest pain.

OBJECTIVE: The objective of the study is to evaluate cardiac risk factors and risk scores for prediction of coronary artery disease (CAD) and adverse outcomes in an emergency department (ED) population judged to be at low to intermediate risk for acute coronary syndrome. METHODS: Informed consent was obtained from consecutive ED patients who presented with chest pain and were evaluated with coronary computed tomography angiography (cCTA). Cardiac risk factors, clinical presentation, electrocardiogram, and laboratory studies were recorded; the Thrombolysis in Myocardial Infarction (TIMI) and Global Registry of Acute Coronary Events (GRACE) scores were tabulated. Coronary computed tomography angiography findings were rated on a 6-level plaque burden scale and classified for significant CAD (stenosis ≥50%). Adverse cardiovascular outcomes were recorded at 30 days. RESULTS: Among 250 patients evaluated by cCTA, 143 (57%) had no CAD, 64 (26%) demonstrated minimal plaque (70% stenosis). Six patients developed adverse cardiovascular outcomes. Among traditional cardiac risk factors, only age (older) and sex (male) were significant independent predictors of CAD. Correlation with CAD was poor for the TIMI (r = 0.12) and GRACE (r = 0.09-0.23) scores. The TIMI and GRACE scores were not useful to predict adverse outcomes. Coronary computed tomography angiography identified severe CAD in all subjects with adverse outcomes. CONCLUSION: Among ED patients who present with chest pain judged to be at low to intermediate risk for acute coronary syndrome, traditional risk factors are not useful to stratify risk for CAD and adverse outcomes. Coronary computed tomography angiography is an excellent predictor of CAD and outcome

Response time patterns for word production and word selection anomias

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Mixed-valent molecular triple-deckers

Two phenothiazine (PTZ) moieties were connected via naphthalene spacers to a central arene to result in stacked PTZ‐arene‐PTZ structure elements. Benzene and tetramethoxybenzene units served as central arenes mediating electronic communication between the two PTZ units. Based on cyclic voltammetry, UV/Vis‐NIR absorption, EPR spectroscopy, and computational studies, the one‐electron oxidized forms of the resulting compounds behave as class II organic mixed‐valence species in which the unpaired electron is partially delocalized over both PTZ units. The barrier for intramolecular electron transfer depends on the nature of the central arene sandwiched between the two PTZ moieties. These are the first examples of rigid organic mixed‐valent triple‐decker compounds with possible electron‐transfer pathways directly across a stacked structure, and they illustrate the potential of oligo‐naphthalene building blocks for long‐range electron transfer and a future molecular electronics technology

Chiral macrocyclic terpyridine complexes

The syntheses of novel chiral M( II ) bis(terpyridine) cage complexes Fe(L1) 2 -c and Ru(L1) 2 -c are described. The extraordinary design of the precursors Fe(L1) 2 and Ru(L1) 2 allows perfect preorganization for the final closing step. Due to the rigidity of the spacers between the two terpyridine moieties, the two isolated enantiomers barely racemize at room temperature in solution. The stable and axially chiral bis(terpyridine) Fe( II ) and Ru( II ) complexes were fully characterized by NMR-spectroscopy, UV-Vis spectroscopy, electrochemical measurements, high resolution mass spectrometry, circular dichroism measurements, and X-ray structural analysis

The Amidase Domain of Lipoamidase Specifically Inactivates Lipoylated Proteins In Vivo

BACKGROUND:In the 1950s, Reed and coworkers discovered an enzyme activity in Streptococcus faecalis (Enterococcus faecalis) extracts that inactivated the Escherichia. coli and E. faecalis pyruvate dehydrogenase complexes through cleavage of the lipoamide bond. The enzyme that caused this lipoamidase activity remained unidentified until Jiang and Cronan discovered the gene encoding lipoamidase (Lpa) through the screening of an expression library. Subsequent cloning and characterization of the recombinant enzyme revealed that lipoamidase is an 80 kDa protein composed of an amidase domain containing a classic Ser-Ser-Lys catalytic triad and a carboxy-terminal domain of unknown function. Here, we show that the amidase domain can be used as an in vivo probe which specifically inactivates lipoylated enzymes. METHODOLOGY/PRINCIPAL FINDINGS:We evaluated whether Lpa could function as an inducible probe of alpha-ketoacid dehydrogenase inactivation using E. coli as a model system. Lpa expression resulted in cleavage of lipoic acid from the three lipoylated proteins expressed in E. coli, but did not result in cleavage of biotin from the sole biotinylated protein, the biotin carboxyl carrier protein. When expressed in lipoylation deficient E. coli, Lpa is not toxic, indicating that Lpa does not interfere with any other critical metabolic pathways. When truncated to the amidase domain, Lpa retained lipoamidase activity without acquiring biotinidase activity, indicating that the carboxy-terminal domain is not essential for substrate recognition or function. Substitution of any of the three catalytic triad amino acids with alanine produced inactive Lpa proteins. CONCLUSIONS/SIGNIFICANCE:The enzyme lipoamidase is active against a broad range of lipoylated proteins in vivo, but does not affect the growth of lipoylation deficient E. coli. Lpa can be truncated to 60% of its original size with only a partial loss of activity, resulting in a smaller probe that can be used to study the effects of alpha-ketoacid dehydrogenase inactivation in vivo