SINBAD, a brilliant IR source from the DAPhiNE storage ring.

SINBAD is the Italian IR synchrotron radiation beamline, designed to work at wavelengths greater than 10 micro m. It is being installed on DAPhiNE, a new collider that is designed to work at 0.51 GeV with a beam current up to 5 A. Due to such a high current, the IR extracted from a bending magnet will be more brilliant than that of a black body at 2000 K by two orders of magnitude at 100 micro m. The beamline optical system, projected by ray-tracing simulation, consists of six mirrors that first focus the radiation on a wedged CVD diamond-film window and then transfer the collimated beam to the experimental area where a Michelson interferometer will be installed.

Mammography with synchrotron radiation.

PURPOSE: To determine the feasibility of using synchrotron radiation (SR) in diagnostic mammography. MATERIALS AND METHODS: Monochromatic SR of x-ray beams of selected energies of 14-20 keV were used to obtain mammograms of surgically removed breast specimens that contained tumor nodules. For comparison, conventional mammograms of the same specimens were also obtained. RESULTS: The mammograms obtained with SR had higher contrast and better resolution than did traditional mammograms and demonstrated excellent detail in all cases studied. The mean glandular doses at 17 and 18 keV were 1.56 and 0.83 mGy, respectively, which is compatible with the mean value of 1.41 mGy delivered with the conventional grid apparatus. CONCLUSION: SR mammography appears to be a promising diagnostic imaging technique.

[Synchrotron radiation: a new source in x-ray mammography]. / La luce del sincrotrone: una nuova sorgente nella mammografia con raggi X.

This work was aimed at evaluating the image quality obtainable in X-ray mammography using synchrotron radiation monochromatic lines. After a short review of the current mammographic techniques, the main features of synchroton radiation in the X-ray field are analyzed, especially of that emitted by the Adone storage ring. Its features are then compared with the radiation emitted by a Coolidge tube. The experimental unit used in this study, including beamline, monochromator and mammograph, is then described together with the experimental method for carrying out a series of experiments in the mammographic field employing both monochromatic lines (E = 17 keV) and white radiation from conventional sources. The first series of experiments is described, which employed standard phantoms: the dependence of resolution and contrast on both wavelength and thickness of breast specimens is reported. Several mammograms of neoplastic breast specimens were obtained after mastectomy: they were acquired using both synchrotron monochromatic lines and radiation emitted by a conventional tube and employing the same acquisition system. The comparison of the two series of images shows that synchrotron radiation can demonstrate a high number of anatomopathologic details with high definition, contrast and resolution which cannot be obtained by means of a conventional source. Our results appear very promising and suggest synchrotron radiation as the major tool in the early diagnosis of neoplastic breast lesions.

Influence of allosteric effectors on the heme conformation of dromedary ferrous nitrosylhemoglobin detected by XANES spectroscopy.

The changes of the Fe heme-active site conformation of dromedary (Camelus dromedarius) nitrosylhemoglobin (HbNO) induced by inositol hexakisphosphate (IHP) and chlofibric acid (CFA) have been studied by using X-ray absorption near-edge structure (XANES) spectroscopy. Structural information has been determined by multiple scattering analysis of the Fe K-edge XANES spectra. The proximal histidine is found to move away from iron centers by about 0.4 Angstrom on the average over the four hemes upon binding of CFA or stoichiometric amount of IHP. In molar excess of polyanion or in the simultaneous presence of IHP, CFA and chloride, the proximal histidine moves back to a position very close to that observed in pure buffer; yet, the structure modulation induced by the allosteric effectors is not completely reversible. Such findings parallel with the functional properties and the spectroscopic (e.g., EPR and absorbance) characteristics of HbNO.

Influence of globin structure on the heme in dromedary carbonmonoxyhemoglobin.

By use of X-ray absorption near-edge structure (XANES), circular dichroism, and visible absorption spectroscopies, dromedary carbonmonoxyhemoglobin has been characterized structurally and functionally. By consideration of the experimental results the following view emerges: (i) the quaternary structure is not the unique factor determining the tertiary environment around the heme, and (ii) the multiplicity of interactions between hemoglobin and solvent components induces a large number of globin conformations, which somehow affect the conformation of the heme such that the structural parameters (i.e., the doming of porphyrins, the movements of the iron relative to the heme plane, the distortion of the ligand field, and the change in the Fe-C-O angle) can be uncoupled.

Heterogeneity of the isolated subunits of the fetal and adult human hemoglobin in solution, detected by XANES spectroscopy.

Differences in the local structure of the heme in the isolated alpha-, beta- and gamma-chains of the adult and fetal human hemoglobin are detected by XANES (X-ray absorption near-edge structure) spectroscopy. The ligand bonding angle to the iron ion in the ligated forms and the displacement of the Fe respect to the porphyrin plane in the deoxy forms are found to be different for each chain.

Oxygen bonding in human hemoglobin and its isolated subunits: a XANES study.

The X-ray absorption near edge structure (XANES) spectra of the human adult and foetal hemoglobin, of the isolated alpha and beta chains, in the oxygenated forms, and of the oxymyoglobin and carp oxyhemoglobin have been measured at the wiggler beam line of the Frascati Synchrotron radiation facility. The bonding angle of oxygen molecule at the iron site in these hemoproteins in solution, has been measured using the multiple scattering theory for data analysis.

Local Fe site structure in the tense-to-relaxed transition in carp deoxyhemoglobin: a XANES (x-ray absorption near edge structure) study.

The Fe-site structure variation in the transition from the low-affinity tense (T) quaternary structure to the high-affinity relaxed (R) structure in carp deoxyhemoglobin was studied by analysis of multiple scattering resonances in the XANES (x-ray absorption near edge structure) spectra. High signal-to-noise XANES spectra were measured at the Frascati "wiggler" synchrotron radiation facility. We find that the forces on the Fe active site due to the change of quaternary protein conformation do not induce variations greater than 0.01 A in interatomic Fe-N distances, variations greater than 0.1 A in the Fe displacement toward the heme plane, or the "doming" of the heme. The relevance of these results to the mechanism of protein control of ligand binding is discussed.

XANES of carboxy and cyanomet-myoglobin. The role of the distal histidine in the bent Fe-C-O configuration.

The ligand bonding geometry of carboxy- and cyanomet-myoglobin (MbCO and MbCN) has been measured by the XANES method (X-ray Absorption Near Edge Structure). A comparison between the ligand bonding geometry of carboxy- and cyanomet-myoglobin and of chelated protoheme methyl ester shows that the bent Fe-C-O configuration is the same in both systems. Therefore, we suggest that this configuration is not associated with any steric constraint imposed by the side chains of the aminoacid residues at the distal side of the heme pocket.

Changes in Fe site structure from fetal to adult hemoglobin probed by XANES.

Iron X-ray absorption near edge structure (XANES) spectra of human fetal (F) and adult (A) deoxyhemoglobin (deoxyHb) measured at the Frascati synchrotron radiation facility reveal the different geometrical structure of the Fe-porphyrin complexes in the two proteins. By this method, having determined for the first time the variation of atomic positions in fetal and adult hemoglobin in solution (close to the 'in vivo' situation), we give further insight into the structure-function relationship in hemoglobins.

Increase of the Fe effective charge in hemoproteins during oxygenation process.

The x-ray absorption near edge structure (XANES) spectra of hemoglobin and myoglobin have been measured at the wiggler beam line of the Frascati Synchrotron Radiation Facility. The energy shifts of the iron absorption jump edge and the chemical shifts of the bound excited state at threshold of 1s core excitations, going from deoxygenated to oxygenated form, are interpreted as evidence of some increase of the positive effective charge on the iron atom upon oxygenation.

XANES study of iron displacement in the haem of myoglobin.

The XANES (X-ray absorption near edge structure) spectra of deoxy human adult haemoglobin (HbA) and myoglobin (Mb) have been measured at the wiggler beam line of the Frascati synchrotron radiation facility. The XANES are interpreted by the multiple scattering cluster theory. The variations in the XANES between HbA and Mb are assigned to changes in the Fe-porphyrin geometry.