Electroplated CoPt magnets for actuation of stiff cantilevers.

A cantilever has been microfabricated for use in non-contact Atomic Force Microscopy (AFM) using a very thick magnetic film to actuate the cantilever motion. The thick magnetic block is deposited electrochemically over a defined area of the cantilever. This cantilever is particularly suitable for driving stiff AFM cantilevers in a liquid environment. Clean mechanical resonances are easily observed. Examples are given of a hard (CoPt) magnet of dimension 29 × 21 × 6 µm(3) electroplated on Silicon cantilevers of stiffness ~22 N/m, giving a static displacement of ~0.2 nm in an applied field of 10(-3) T.

Solvation and squeeze out of hexadecane on graphite.

We have performed simultaneous force and conductivity measurement of hexadecane liquid confined between a conducting atomic force microscope tip and a graphite surface. Both the current and the force data reveal discrete solvation layering of the hexadecane near the surface. We typically observe that the current does not vary with load in a simple way as the layer closest to the surface is compressed, but increases markedly prior to the expulsion of material from the tip-sample gap. We infer that even for a nanoscale asperity there is conformation change of the confined hexadecane under the tip apex prior to squeeze out of the molecules.

Tryptophan and tyrosine radicals in ribonucleotide reductase: a comparative high-field EPR study at 94 GHz.

Tryptophan radicals, which are generated in the reconstitution reaction of mutants Y122F and Y177W of subunit R2 apoprotein of E. coli and mouse ribonucleotide reductase (RNR), respectively, with Fe(2+) and oxygen, are investigated by high-field EPR at 94 GHz and compared with the tyrosine radicals occurring in the respective wild-type proteins. For the first time, accurate g-values are obtained for protein-associated neutral tryptophan free radicals, which show only a small anisotropy. The apparent hyperfine patterns observed in frozen solutions are very similar for tryptophan and tyrosine radicals in mouse subunit R2 at conventional X-band EPR. The radicals can, however, be discriminated by their different g-tensors using high-field EPR. Tryptophan radicals were postulated as reaction intermediates in the proposed radical transfer pathway of RNR. Furthermore, the data obtained here for the electronic structure of protein-associated tryptophan neutral free radicals are important for identification and understanding of the functional important tryptophan radicals which occur in other enzymes, e.g., DNA photolyase and cytochrome c peroxidase, where they are magnetically coupled to other radicals or to a metal center.

Photosystem II single crystals studied by EPR spectroscopy at 94 GHz: the tyrosine radical Y(D)(*).

Electron paramagnetic resonance (EPR) spectroscopy at 94 GHz is used to study the dark-stable tyrosine radical Y(D)(*) in single crystals of photosystem II core complexes (cc) isolated from the thermophilic cyanobacterium Synechococcus elongatus. These complexes contain at least 17 subunits, including the water-oxidizing complex (WOC), and 32 chlorophyll a molecules/PS II; they are active in light-induced electron transfer and water oxidation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with four PS II dimers per unit cell. High-frequency EPR is used for enhancing the sensitivity of experiments performed on small single crystals as well as for increasing the spectral resolution of the g tensor components and of the different crystal sites. Magnitude and orientation of the g tensor of Y(D)(*) and related information on several proton hyperfine tensors are deduced from analysis of angular-dependent EPR spectra. The precise orientation of tyrosine Y(D)(*) in PS II is obtained as a first step in the EPR characterization of paramagnetic species in these single crystals.

A novel approach to separating EPR lines arising from species with different transition moments.

In pulsed EPR, spectral contributions from several species in one sample can be separated based on different EPR transition probabilities. This is usually done by monitoring the Rabi nutations in a 2D experiment. By using long pulses, the FID and echo shapes of species with different transition probabilities differ significantly, including temporal shifts of the observed echo signals in a two-pulse ESE experiment. These shifts can be used to disentangle spectral components in a 1D field-swept ESE experiment by choosing an appropriate detection time. This approach is demonstrated by experiments on a sample containing Mn(2+) and Cr(3+) centers as well as on an exchange-coupled Mn(III)/Mn(IV) system with Mn(2+) contaminations.