High--quality single crystals of the heavy fermion superconductors CeCoIn$_5$ and CeIrIn$_5$ have been studied by means of low--temperature Scanning Tunneling Microscopy. Methods were established to facilitate textit{in-situ} sample cleaving. Spectro
scopy in CeCoIn$_5$ reveals a gap which persists to above $T_c$, possibly evidencing a precursor state to SC. Atomically resolved topographs show a rearrangement of the atoms at the crystal surface. This modification at the surface might influence the surface properties as detected by tunneling spectroscopy.
FoF1-ATP synthase is the enzyme that provides the chemical energy currency adenosine triphosphate, ATP, for living cells. The formation of ATP is accomplished by a stepwise internal rotation of subunits within the enzyme. Briefly, proton translocatio
n through the membrane-bound Fo part of ATP synthase drives a 10-step rotary motion of the ring of c subunits with respect to the non-rotating subunits a and b. This rotation is transmitted to the gamma and epsilon subunits of the F1 sector resulting in 120 degree steps. In order to unravel this symmetry mismatch we monitor subunit rotation by a single-molecule fluorescence resonance energy transfer (FRET) approach using three fluorophores specifically attached to the enzyme: one attached to the F1 motor, another one to the Fo motor, and the third one to a non-rotating subunit. To reduce photophysical artifacts due to spectral fluctuations of the single fluorophores, a duty cycle-optimized alternating three-laser scheme (DCO-ALEX) has been developed. Simultaneous observation of the stepsizes for both motors allows the detection of reversible elastic deformations between the rotor parts of Fo and F1.
Confocal time resolved single-molecule spectroscopy using pulsed laser excitation and synchronized multi channel time correlated single photon counting (TCSPC) provides detailed information about the conformational changes of a biological motor in re
al time. We studied the formation of adenosine triphosphate, ATP, from ADP and phosphate by FoF1-ATP synthase. The reaction is performed by a stepwise internal rotation of subunits of the lipid membrane-embedded enzyme. Using fluorescence resonance energy transfer, FRET, we detected rotation of this biological motor by sequential changes of intramolecular distances within a single FoF1-ATP synthase. Prolonged observation times of single enzymes were achieved by functional immobilization to the glass surface. The stepwise rotary subunit movements were identified by Hidden Markov Models (HMM) which were trained with single-molecule FRET trajectories. To improve the accuracy of the HMM analysis we included the single-molecule fluorescence lifetime of the FRET donor and used alternating laser excitation to co-localize the FRET acceptor independently within a photon burst. The HMM analysis yielded the orientations and dwell times of rotary subunits during stepwise rotation. In addition, the action mode of bactericidal drugs, i.e. inhibitors of FoF1-ATP synthase like aurovertin, could be investigated by the time resolved single-molecule FRET approach.
High resolution topographic images obtained by scanning tunneling microscope in the insulating state of Pr0.68Pb0.32MnO3 single crystals showed regular stripe-like or zigzag patterns on a width scale of 0.4 - 0.5 nm confirming a high temperature pola
ronic state. Spectroscopic studies revealed inhomogeneous maps of zero-bias conductance with small patches of metallic clusters on length scale of 2 - 3 nm only within a narrow temperature range close to the metal-insulator transition. The results give a direct observation of polarons in the insulating state, phase separation of nanometer-scale metallic clusters in the paramagnetic metallic state, and a homogeneous ferromagnetic state.
