Magnetic excitations and phase transition of CsFeBr3 in an external magnetic field

In CSFeBr₃ the Fe²⁺ ion with effective spin one has locally a singlet ground state (m=0). The antiferromagnetic interactions between neighbouring Fe-ions are too weak as compared with the anisotropy constant to introduce long range order in the absence of an external field. By inelastic neutron scattering we studied the magnetic excitations in an external magnetic field up to 5 Tesla applied along thec-axis. A linear Zeeman splitting was observed with a Landé factorg=2.4. The field renormalizes the dispersion curves in such a way that the exchange interaction has decreasing influence with increasing field. Theoretical calculations according to the excitonic model of Lindgård describe the experimental results very well. At 4.1 Tesla a phase transition appears to a commensurate long range order with a 120° arrangement of the spins in the hexagonal plane. Within the limits of experimental observation this phase transition has no influence on the dynamical behaviour. No critical phenomena could be observed. The dynamical structure factor |G _j()|² of the lower Zeeman split modes decreases with increasing field.     

Magnetic excitations in the quasi one-dimensional antiferromagnetic singlet groundstate system CsFeBr3

We have measured the magnetic excitations in CsFeBr₃ along the chain direction (z-axis) and perpendicular to it by inelastic neutron scattering. The measured dispersion curves can be reproduced by the formula $$\omega ^2 (q) = A^2 - 8A[J\cos (\pi q_c ) + J'\gamma (2\pi q_ \bot )]R(T)$$ which is very different from dispersion relations for usual 1 D antiferromagnets, because of the singlet groundstate of this system. The large value of the anisotropy energyA/k=29.8±0.5 K, which is independent of temperature, causes the singlet groundstate. The intra-and inter-chain exchange parameters areJ/k=?3.2±0.15K andJ'/k=?0.32±0.02 K determined atT=1.4 K. At 1.4 K the renormalisation factor is taken to beR(T)=1. AtT=30 K the value forR(T) was found to be 0.5±0.1 keepingJ andJ' unchanged. The excitations at (1/3 1/31) show soft mode behaviour but no phase transition. The observed intensities are interpreted by a heuristic model for the eigenvectors in the excited state including antiferro-as well as ferromagnetic configurations of the fluctuations.     

Patents and literature

Protein engineering and site-directed mutagenesis is becoming immensely important in both fundamental studies and commercial applications involving proteins and enzymes in biocatalysis. Protein engineering has become a powerful tool to help biochemists and molecular enzymologists elucidate structure-function relationships in enzymic active sites, to understand the intricacies of protein folding and denaturation, and to alter the selectivity of enzymatic catalysis. Commercial applications of engineered enzymes are being developed to increase protein stability, widen or narrow substrate specificity, and to develop novel approaches for use of enzymes in organic synthesis, drug design, and clinical applications. In addition to protein engineering, novel expression systems have been designed to prepare large quantities of genetically engineered proteins. Recent US patents and scientific literature on protein engineering, site-directed mutagenesis, and protein expression systems related to protein engineering are surveyed. Patent abstracts are summarized individually and a list of literature references are given.     

CHEMICALLY MODIFIED PHOTOSYNTHETIC BACTERIAL REACTION CENTERS: CIRCULAR DICHROISM, RAMAN RESONANCE, LOW TEMPERATURE ABSORPTION, FLUORESCENCE AND ODMR SPECTRA AND POLYPEPTIDE COMPOSITION OF BOROHYDRIDE TREATED REACTION CENTERS FROM Rhodobacter sphaeroides R26

Abstract— Reaction centers from Rhodobacter sphaeroides have been modified by treatment with sodium borohydride similar to the original procedure [Ditson et al., Biochim. Biophys. Acta 766 , 623 (1984)], and investigated spectroscopically and by gel electrophoresis.
(1) Low temperature (1.2 K) absorption, fluorescence, absorption- and fluorescence-detected ODMR, and microwave-induced singlet-triplet absorption difference spectra (MIA) suggest that the treatment produces a spectroscopically homogeneous preparation with one of the 'additional' bacteriochlorophylls being removed. The modification does not alter the zero field splitting parameters of the primary donor triplet (^TP870).
(2) From the circular dichroism and Raman resonance spectra in the1500–1800 cm^-1 region, the removed pigment is assigned to Bchl_M, e.g. the "extra" Bchl on the "inactive" M-branch.
(3) A strong coupling among all pigment molecules is deduced from the circular dichroism spectra, because pronounced band-shifts and/or intensity changes occur in the spectral components assigned to all pigments. This is supported by distinct differences among the MIA spectra of untreated and modified reaction centers, as well as by Raman resonance.
(4) The modification is accompanied by partial proteolytic cleavage of the M-subunit. The preparation is thus spectroscopically homogeneous, but biochemically heterogenous.     

1H- and 13C-NMR. Studies of some metal complexes of o,o′-dihydroxyazobenzenes

The aromatic ¹H- and ¹³C-NMR. spectra of some metal complexes of o, o′-dihydroxyazobenzenes are shown to be useful in distinguishing the two possible isomers (acolar and discolar) stemming from the non equivalence of the two ligating azo nitrogen atoms. The ortho aromatic carbon atoms, C(6) and C(12) experience relatively large upfield shifts between 12.8 and 15.7 ppm when the adjacent nitrogen atom is coordinated. The protons attached to these carbon atoms are shifted downfield. The values ⁿJ (¹⁵N, ¹³C) for the ligand 2,2′-dihydroxy-3-methyl-4′-chloro-5-(t-butyl)-¹⁵N-azobenzene are reported.