Optochemical sensing by immobilizing fluorophore-encapsulating liposomes in sol–gel thin films

The chemical stability of optochemical sensors depends largely on the physiochemical properties of the supportive matrix of the sensor and on the method used to immobilize sensing reagents to the supportive matrix of the sensor. Leaking of physically immobilized sensing reagents from the matrix support decreases the stability of the sensor and its overall usefulness. Covalent immobilization eliminates leakage of the sensing reagent from the support but may lead to alteration of spectral properties and loss of analyte response. This paper presents a new method for physical immobilization of polar fluorescence dyes in a sensing support. The method is based on the immobilization of fluorescent dye encapsulating liposomes in a sol–gel film of micrometer thickness. The encapsulation of the dye molecules in the liposomes effectively increases the molecular dimensions of the sensing reagent, thus preventing its leakage from the matrix support. This paper describes the analytical properties of a pH sensor fabricated by immobilizing carboxyfluorescein-encapsulating liposomes in a sol–gel thin film. The sensor shows excellent stability with respect to dye leaking which in turn leads to high reproducibility and sensitivity of about 0.01 pH units. The linear dynamic range of the sensor is between pH 6 and 7.5 and its response time is at the sub-seconds time scale.     

Quantum Unique Ergodicity for Maps on the Torus

When a map is classically uniquely ergodic, it is expected that its quantization will posses quantum unique ergodicity. In this paper we give examples of Quantum Unique Ergodicity for the perturbed Kronecker map, and an upper bound for the rate of convergence. submitted 3/02/05, accepted 20/10/05     

A framework for the value of information in inventory replenishment

Technological advances and changes in supply chain management practices have combined to draw attention to the value of information sharing in inventory replenishment. Academic research has produced seemingly conflicting results due to differences in the type of information that is shared, the supply chain structure, and the selection and parameterization of performance goals. This research provides a framework to help explain apparent differences in the extant literature. Our purpose is to understand what determines the value of information. With this specific view, we establish a set of research questions and suggest directions for future research.     

Evidence that the β subunit of Chlamydia trachomatis ribonucleotide reductase is active with the manganese ion of its manganese(IV)/iron(III) cofactor in site 1

The reaction of a class I ribonucleotide reductase (RNR) begins when a cofactor in the β subunit oxidizes a cysteine residue ~35 ? away in the α subunit, generating a thiyl radical. In the class Ic enzyme from Chlamydia trachomatis (Ct), the cysteine oxidant is the Mn(IV) ion of a Mn(IV)/Fe(III) cluster, which assembles in a reaction between O(2) and the Mn(II)/Fe(II) complex of β. The heterodinuclear nature of the cofactor raises the question of which site, 1 or 2, contains the Mn(IV) ion. Because site 1 is closer to the conserved location of the cysteine-oxidizing tyrosyl radical of class Ia and Ib RNRs, we suggested that the Mn(IV) ion most likely resides in this site (i.e., (1)Mn(IV)/(2)Fe(III)), but a subsequent computational study favored its occupation of site 2 ((1)Fe(III)/(2)Mn(IV)). In this work, we have sought to resolve the location of the Mn(IV) ion in Ct RNR-β by correlating X-ray crystallographic anomalous scattering intensities with catalytic activity for samples of the protein reconstituted in vitro by two different procedures. In samples containing primarily Mn(IV)/Fe(III) clusters, Mn preferentially occupies site 1, but some anomalous scattering from site 2 is observed, implying that both (1)Mn(II)/(2)Fe(II) and (1)Fe(II)/(2)Mn(II) complexes are competent to react with O(2) to produce the corresponding oxidized states. However, with diminished Mn(II) loading in the reconstitution, there is no evidence for Mn occupancy of site 2, and the greater activity of these "low-Mn" samples on a per-Mn basis implies that the (1)Mn(IV)/(2)Fe(III)-β is at least the more active of the two oxidized forms and may be the only active form.     

Evidence for oxygen binding at the active site of particulate methane monooxygenase

Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that converts methane to methanol in methanotrophic bacteria. The enzyme consists of three subunits, pmoB, pmoA, and pmoC, organized in an α(3)β(3)γ(3) trimer. Studies of intact pMMO and a recombinant soluble fragment of the pmoB subunit (denoted as spmoB) indicate that the active site is located within the soluble region of pmoB at the site of a crystallographically modeled dicopper center. In this work, we have investigated the reactivity of pMMO and spmoB with oxidants. Upon reduction and treatment of spmoB with O(2) or H(2)O(2) or pMMO with H(2)O(2), an absorbance feature at 345 nm is generated. The energy and intensity of this band are similar to those of the μ-η(2):η(2)-peroxo-Cu(II)(2) species formed in several dicopper enzymes and model compounds. The feature is not observed in inactive spmoB variants in which the dicopper center is disrupted, consistent with O(2) binding to the proposed active site. Reaction of the 345 nm species with CH(4) results in the disappearance of the spectroscopic feature, suggesting that this O(2) intermediate is mechanistically relevant. Taken together, these observations provide strong new support for the identity and location of the pMMO active site.     

Dual topological unitarization: An ordered approach to Hadron theory

A review is given of developments between 1973 and 1977 that have added the concept of order to general S-matrix principles with the aim of constructing a bootstrap theory of hadrons.     

Observation of anomalously large spectral bandwidth in a high-gain self-amplified spontaneous emission free-electron laser

Observation of ultrawide bandwidth, up to 15% full-width, high-gain operation of a self-amplified spontaneous emission free-election laser (SASE FEL) is reported. This type of lasing is obtained with a strongly chirped beam (deltaE/E approximately 1.7%) emitted from the accelerator. Because of nonlinear pulse compression during transport, a short, high current bunch with strong mismatch errors is injected into the undulator, giving high FEL gain. Start-to-end simulations reproduce key features of the measurements and provide insight into mechanisms, such as angular spread in emitted photon and electron trajectory distributions, which yield novel features in the radiation spectrum.     

Experimental characterization of nonlinear harmonic radiation from a visible self-amplified spontaneous emission free-electron laser at saturation

Nonlinear harmonic radiation was observed using the VISA self-amplified, spontaneous emission (SASE) free-electron laser (FEL) at saturation. The gain lengths, spectra, and energies of the three lowest SASE FEL modes were experimentally characterized. The measured nonlinear harmonic gain lengths and center spectral wavelengths decrease with harmonic number, n, which is consistent with nonlinear harmonic theory. Both the second and third nonlinear harmonics energies are about 1% of the fundamental energy. These experimental results demonstrate for the first time the feasibility of using nonlinear harmonic SASE FEL radiation to produce coherent, femtosecond x rays.