PubMed Health⌕ Search

Biomedical subjects

S Morante

Publications and source records attributed to S Morante.

28 records · Page 2Linked to original sources
PubMed1987

Studies on the linkage between spin equilibria and protein structure in carp ferric hemoglobin.

The effects of protein conformation on the spin-state equilibria of several derivatives of carp hemoglobin have been examined. This has been done by measuring the pH dependence of the paramagnetic susceptibilities of these derivatives in the presence and absence of inositol hexakisphosphate, P6-inositol. In all cases the addition of P6-inositol at low pH and the lowering of the pH in the presence of P6-inositol shift the spin-state equilibrium in favor of the high-spin electronic configuration. The P6-inositol and pH dependence of these magnetic properties parallels the pH and P6-inositol dependence of the conformational state of the hemoglobin as determined in earlier studies and further supports a thermodynamic linkage between the electronic state of the iron atoms and the quaternary structure of the hemoglobin molecule.

Animals↗
PubMed1986

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.

Animals↗
PubMed1985

Reexamination of the evidence for paramagnetism in oxy- and carbonmonoxyhemoglobins.

Experiments have been carried out in an attempt to confirm previous reports of paramagnetism in the oxy- and carbonmonoxy derivatives of human and carp hemoglobin. When care is taken to ensure complete saturation of the hemoglobins with ligand and the diamagnetic contributions of all of the buffers are carefully evaluated, these hemoglobin derivatives are found to have the same gram susceptibilities as exhibited by a set of metal free proteins, suggesting that they are fully diamagnetic.

Animals↗
PubMed1983

Quaternary structure and spin equilibria in ferric hemoglobins. A room temperature study.

The effective magnetic moments for a number of human and carp methemoglobin derivatives were determined in solution at room temperature. The data permit us to confirm the dependence of the spin-state equilibrium of azide methemoglobin on the quarternary state of the hemoglobin and to demonstrate a similar dependence for both human and carp aquomethemoglobin. In addition, the pH dependence of the effective magnetic moment and the Soret spectrum of carp azidemethemoglobin are compared.

Animals↗
PubMed1983

Magnetic and spectral properties of carp carbonmonoxyhemoglobin. Competitive effects of chloride ions and inositol hexakisphosphate.

We have extended our studies on the magnetic properties of carp carbonmonoxyhemoglobin and the dependence of these properties upon solution variables. Using an improved version of the superconducting magnetometer, we have found that the magnetic susceptibility of carp carbonmonoxyhemoglobin is sensitive to both inositol hexakisphosphate and chloride ion. The dependence upon chloride ion concentration is complex. At relatively low concentrations this anion reverses the effect of inositol hexakisphosphate, restoring paramagnetism. At higher chloride concentrations the protein is converted to a roughly diamagnetic state in the absence of inositol hexakisphosphate. Along with these susceptibility studies, we have examined the effects of these anions on other properties of carp carbonmonoxyhemoglobin. The positions of the Soret bands of human and carp methemoglobin derivatives are correlated with spin state; changes in the magnetic susceptibility of carbonmonoxyhemoglobin are similarly associated with alterations in this spectral band. We have also examined the effects of these anions on the proton nuclear magnetic resonance spectrum of carp carbonmonoxyhemoglobin. Both chloride and inositol hexakisphosphate alter the position of the proton resonances in the ring-current-shifted region of the spectrum.

Animals↗
PubMed1983

X-ray absorption near edge structure (XANES) for CO, CN and deoxyhaemoglobin: geometrical information.

We use the recently developed multiple scattering theory to give a quantitative analysis of the X-ray absorption near edge structure (XANES) of haemoglobin and some of its substituents. We demonstrate that the XANES may contain information not provided by the extended X-ray absorption fine structure (EXAFS) part of the spectrum about the coordination geometry around the Fe atom, and in particular discuss the sensitivity of the XANES to the orientation of the CN group in HbCN. The anisotropy of the system leads to a strong dependence of the calculated spectrum on the polarisation of the X-rays. We show how this effect can be exploited in further XANES structural studies.

Carboxyhemoglobin↗
PubMed1980

Magnetic equivalence of the hemes in hemoglobin Zürich.

The magnetic susceptibilities of solutions of deoxyhemoglobin Zürich and deoxyhemoglobin A have been found quite close together, in contrast to previous findings. Therefore, any magnetic inequivalence between alpha- and beta-hemes must be confined to finer details.

Heme↗
PubMed1980

Variability of the magnetic moment of carbon monoxide hemoglobin from carp.

Deionized carp carbon monoxide hemoglobin in distilled water or in bis(2-hydroxyethyl)imino-tris(hydroxymethyl)methane or Tris buffer exhibits a slight but significant paramagnetism. This is most clearly demonstrated by the decrease in this paramagnetism that is caused by the addition of inositol hexaphosphate to this protein in the former buffer at pH 6.3-6.4. No such effect is seen when inositol hexaphosphate is added to carp cyanomethemoglobin, demonstrating that the change observed with carbon monoxide derivative is not due to a modification in the diamagnetic properties of the protein.

Animals↗
PubMed1978

Room-temperature magnetic properties of oxy- and carbonmonoxyhemoglobin.

The magnetic susceptibility and the density of human oxy-(HbO(2)) and carbonmonoxyhemoglobin (HbCO) solutions of various concentrations have been measured at room temperature, with pure water used as a calibrant. Solutions of unstripped and stripped HbO(2) at pH 7.2 in unbuffered water solvent were always found to be less diamagnetic than pure water, whereas solutions of HbCO in identical conditions were always found to be more diamagnetic than pure water. After correcting for concentration-dependent density changes and assuming the HbCO samples to be fully diamagnetic, the paramagnetic reduction of the diamagnetic susceptibility of HbO(2) corresponds to a molar susceptibility per heme (chi(M) (heme)) of 2460 +/- 600 x 10(-6) cgs/mol.

Journal Article↗