Assignment of conformation-sensitive near-infrared bands in high-spin ferrous haemoproteins. Low-temperature magnetic circular dichroism data

An assignment of the near-infrared bands in the 600–800 nm spectral region observed in magnetic circular dichroism (MCD) spectra of high-spin ferrous haemoproteins is presented. The assignment is based on a relative energy level scheme for iron d-electrons, a comparison of predicted and measured temperature dependences of MCD intensity, a sign of MCD bands and a group theoretical analysis of allowed transitions. The proposed assignment is consistent with the ∼15-nm red shift of the ∼760 nm band on breakage of the Fe-His bond in deoxy-myoglobin at low pH, with low-temperature photolysis experiments available for CO complexes of several haemoproteins. In accordance with the observations, the intensity of the MCD bands for proteins with a sulphur anion of cysteine as proximal haemligand (cytochrome P450 and chloroperoxidase) is predicted to be diminished by at least one order of magnitude compared to that for proteins with an imidazole of a histidine as a protein-derived haemligand (i.e. myoglobin, haemoglobin and horseradish peroxidase). Received: 4 February 1997 / Accepted: 1 May 1997     

Calorimeter energy calibration using the energy conservation law

A new calorimeter energy calibration method was developed for the proposed ILC detectors. The method uses the center-of-mass energy of the accelerator as the reference. It has been shown that using the energy conservation law it is possible to make ECAL and HCAL cross calibration to reach a good energy resolution for the simple calorimeter energy sum.      

Extending physics capabilities of the PHENIX detector with calorimetry at forward rapidities

The PHENIX detector at RHIC has been designed to study different signatures of the states of matter created in heavy-ion collisions, and to investigate the spin structure of the nucleon. The PHENIX detector measures muons in two muon spectrometers, located at forward rapidities (1.2 < |η| < 2.4) and hadrons, electrons and photons in the two central spectrometers at midrapidity (|η| <0.35). To make a next step in the PHENIX research program, it is necessary to extend the rapidity coverage beyond the limits set by the existing central spectrometer. The functionality of the PHENIX muon detectors can be extended with added capabilities to measure photonic and hadronic jets. Tungsten calorimeters with silicon pixel readout and fine transverse and longitudinal segmentation are proposed to attain this goal. The proposed calorimeters will be located in the forward directions on either side of the PHENIX interaction point. In this talk we report on the studies of the functionality of the proposed calorimeters: the detector energy resolution, the jet reconstruction capabilities and the characteristics of pion rejection.     

Invariant integrals in continuum mechanics

Presented at the International Conference on Contemporary Mathematical Problems in Mechanics and Their Applications (Moscow, November 11–15, 1987).     

Approximation by translates of refinable functions

Summary. The functions are refinable if they are combinations of the rescaled and translated functions . This is very common in scientific computing on a regular mesh. The space of approximating functions with meshwidth is a subspace of with meshwidth . These refinable spaces have refinable basis functions. The accuracy of the computations depends on , the order of approximation, which is determined by the degree of polynomials that lie in . Most refinable functions (such as scaling functions in the theory of wavelets) have no simple formulas. The functions are known only through the coefficients in the refinement equation – scalars in the traditional case, matrices for multiwavelets. The scalar "sum rules" that determine are well known. We find the conditions on the matrices that yield approximation of order from . These are equivalent to the Strang–Fix conditions on the Fourier transforms , but for refinable functions they can be explicitly verified from the . Received August 31, 1994 / Revised version received May 2, 1995     

Phase Equilibria and Crystal Structure of Complex Oxides in the La–Sr–Co–Ni– System

Phase equilibria in the La–Sr–Co–Ni–O system were studied in air at 1100°. The samples for the study were synthesized by the standard ceramic and citrate processes. The limiting solubility and structure of La_1-xSr_xCo_1-yNi_yO_3- and (La_1-xSr_x)₂Co_1-yNi_yO₄ solid solutions were determined by Xray powder diffraction analysis. La_1-xSr_xCo_1-yNi_yO₃- solid solutions with 0 x 0.5 have a distorted rhombohedral perovskitelike structure (R c space group). An increase in the strontium concentration reduces the rhombohedral distortions, and the compounds with x < 0.5 have an ideal cubic structure (Pm3m space group). (La_1-xSr_x)₂Co_1-yNi_yO₄ crystals have a tetragonal K₂NiF₄ type unit cell (I4/mmm space group). The relationships between unit cell parameters and compositions were obtained for singlephase La_1-xSr_xCo_1-yNi_yO_3- and (La_1-xSr_x)₂Co_1-yNi_yO₄ samples. The existence regions of La_1-xSr_xCo_1-yNi_yO₃- and La_1-xSr_x)₂Co_1-yNi_yO₄ solid solutions were distinguished on P–T phase diagrams.     

3-Lithiomethyl-4-phenylsydnone: A new type of organometallic derivatives of sydnones

An α-lithium derivative of 3-alkyl-substituted sydnone was first synthesized by direct metallation of 3-methyl-4-phenylsydnone withn-butyllithium. The reactivity of the compound obtained was studied. Reactions of 3-lithiomethyl-4-phenylsydnone with various electrophiles can serve as a convenient method for preparation of functionalized sydnones.     

The nature of the exchange coupling between high-spin Fe(III) heme o3 and CuBII in Escherichia coli quinol oxidase, cytochrome bo3: MCD and EPR studies

Fully oxidized cytochrome bo3 from Escherichia coli has been studied in its oxidized and several ligand-bound forms using electron paramagnetic resonance (EPR) and magnetic circular dichroism (MCD) spectroscopies. In each form, the spin-coupled high-spin Fe(III) heme o3 and CuB(II) ion at the active site give rise to similar fast-relaxing broad features in the dual-mode X-band EPR spectra. Simulations of dual-mode spectra are presented which show that this EPR can arise only from a dinuclear site in which the metal ions are weakly coupled by an anisotropic exchange interaction of J 1 cm-1. A variable-temperature and magnetic field (VTVF) MCD study is also presented for the cytochrome bo3 fluoride and azide derivatives. New methods are used to extract the contribution to the MCD of the spin-coupled active site in the presence of strong transitions from low-spin Fe(III) heme b. Analysis of the MCD data, independent of the EPR study, also shows that the spin-coupling within the active site is weak with J approximately 1 cm-1. These conclusions overturn a long-held view that such EPR signals in bovine cytochrome c oxidase arise from an S' = 2 ground state resulting from strong exchange coupling (J > 10(2) cm-1) within the active site.