Differential Pulse Polarographic Determination of Nitrate in AUT Solution

A differential pulse polarographic method for the determination of nitrate ion has been developed. With 0.5 M CaCl₂ as supporting electrolyte, NO^?₃ is reduced to give a peak with E_1/2=–1.836 Volt vs. the Ag/AgCl electrode. The differential pulse polarographic peak height is proportional to the nitrate concentration from 20 to 60 ppm. The detection limit for nitrate is 2 ppm in pure aqueous solution. In the determination of 40 ppm nitrate a relative precision (relative standard deviation) of less than 2% was achieved. Nitrite interferes seriously and should be absent if accurate results are required. The method has been applied to the determination of nitrate in Ammonium Uranyl Tricarbonate (AUT) Solution, results obtained by this method are compared to those obtained by ion chromatography. The agreement between the two sets of results suggests that the DPP method can be used with a fair degree of confidence.     

Investigation of the Doughnut Effect in Cy3-Labeled Protein Microarrays using Scanning Near-Field Optical Microscope

We demonstrate the fluorescence mapping of protein microarrays by the technique of scanning near-field optical microscopy (SNOM) and confocal microscopy. Micron sized spots (300 μm) of human Immunoglobulin G (hIgG) protein with and without a Cy3 dye labeling have been fabricated on glass substrates by an immobilization method which makes use of calixcrown derivatives termed Prolinker. We have also tried to probe into the well-known “doughnut effect” observed in fluorescence images of proteins using the SNOM technique. The topographic and fluorescence SNOM images revealed that the number of proteins at the boundary of the spot were more than at the center in the case of the microarray spot which showed brighter luminescence at the edge than at the center in the confocal image.     

Femtosecond transform-limited Kerr-lens mode-locked dye lasers

Using SF6 glass plates as intracavity Kerr lenses and double-prism pairs for dispersion compensation, we achieve tunable femtosecond passive mode locking in rhodamine 590 (R6G) and 4-dicyanomethylene-2-methyl-16-p-dimethylaminostyryl-4H-pyran (DCM) dye lasers. The R6G laser produces transform limited 240–500 fs pulses between 577 and 606 nm, and the DCM laser produces 150 fs transform-limited pulses between 650 and 671 nm. We use dilute intracavity saturable-absorber jets to make the mode locking self-starting. Characteristics of the pulses and the stability regions of the lasers agree with general theories of passive mode locking.     

A high-gain porous silicon metal–semiconductor–metal photodetector through rapid thermal oxidation and rapid thermal annealing

2 tungsten lamp at 1.83 mA excited by a 0.85-mW 675-nm laser diode. We also demonstrate that the dark current could be greatly reduced through rapid thermal oxidation and rapid thermal annealing. Received: 4 August 1997/Accepted: 28 May 1998     

Investigation by EPR and ENDOR spectroscopy of the novel 4Fe ferredoxin fromPyrococcus furiosus

The hyperthermophilic archaeonPyrococcus furiosus contains a four-Fe ferredoxin (Pf- Fd) that differs from most other 4Fe-Fd’s in that its [Fe₄S₄] cluster is anchored to protein by only three cysteinyl residues.Pf- Fd also is of interest because in its reduced form, [Fe₄S₄]⁺, the cluster exhibits bothS = 1/2 andS = 3/2 spin states. Addition of excess cyanide ion converts the cluster exclusively to anS = 1/2 state (g₁ = 2.09, g₂ = 1.95, g₃ = 1.92), however dialysis restores the EPR signal of native reduced protein indicating that the cluster is not irreversibly altered by cyanide. Both the native protein and protein in the presence of excess cyanide ion (Pf- Fd 4Fe-CN) were investigated here using the techniques of electron paramagnetic resonance (EPR) and electron-nuclear double resonance (ENDOR) spectroscopy. In particular,Pf- Fd 4Fe-CN was investigated using¹³CN^? and C¹⁵N^? ligands.¹³C and¹⁵N ENDOR indicated that a single cyanide ion bound directly, with the cluster showing an unusually small contact interaction (a_iso(¹³C)～ ?3 MHz, a_iso(¹⁵N) ～ 0). This is in contrast to cyanide bound to monomeric low-spin Fe(III)-containing proteins such as transferrin and myoglobin, for which the¹³C hyperfine coupling has a large isotropic component (a_iso(¹³C) ≈ ?30 MHz). This small contact interaction is not due to low spin density of Fe, as⁵⁷Fe ENDOR of the singly and triply labeledPf- Fd 4FeCN isotopologs, [⁵⁷FeFe₃S₄]⁺ and [Fe⁵⁷Fe₃S₄]⁺, show hyperfine coupling characteristic for [Fe₄S₄]⁺ clusters, particularly for the Fe to which cyanide binds. Thus, the low spin density on¹³C is not due to low spin density on the Fe ion to which it binds. Further theoretical work is needed to explain the contrast between the strong electronic effect of cyanide ion binding with the low spin density on the ligand.