Structure of the Fe-heme in the hemodimeric hemoglobin from Scapharca inaequivalvis and in the T721 mutant: an X-ray absorption spectroscopic study at low temperature.

The Fe site structure in the recombinant wild-type and T721 mutant of the cooperative homodimeric hemoglobin (HbI) of the mollusc Scapharca itnaequivalvis has been investigated by measuring the Fe K-edge X-ray absorption near edge structure (XANES) spectra of their oxy, deoxy and carbonmonoxy derivatives, and the cryogenic photoproducts of the carbonmonoxy derivatives at T = 12 K. According to our results, the Fe site geometry in T72I HbI-CO is quite similar to that of human carbonmonoxy hemoglobin (HbA-CO), while in native HbI-CO it seems intermediate between that of HbA-CO and sperm whale MbCO. The XANES spectra of oxy and deoxy derivatives are similar to the homologous spectra of human HbA, except for T72I HbI, for which the absorption edge is blue-shifted (about + 1 eV) towards the spectrum of the oxy form.

Stabilization of the T-state of ferrous human adult haemoglobin by chlorpromazine and trifluoperazine.

In the present study, the effect of the neuroleptics chlorpromazine (2-chloro-N,N-dimethyl-10H-phenothiazine-10-propanamine) and trifluoperazine {10-[3-(4-methylpiperazin-l-yl)-propyl]-2-trifluoromethyl)-10-H- [phenothiazine}-10H-phenothiazine¿ on the EPR-spectroscopic properties of ferrous human adult nitrosylated haemoglobin (HbNO) is reported. Addition of the two drugs to HbNO shifted the conformational equilibrium from the high- to the low-affinity form of the ligated tetramer, as observed for 2,3-D-glycerate bisphosphate, the physiological modulator of haemoglobin action. The effect of chlorpromazine and trifluoperazine on the EPR-spectroscopic properties of HbNO was enhanced by inositol hexakisphosphate.

Stabilization of the T-state of human hemoglobin by proflavine, an antiseptic drug.

The effect of proflavine (3,6-diaminoacridine), an antiseptic drug, on the spectroscopic and oxygen binding properties of ferrous human adult hemoglobin (Hb) has been investigated. Upon binding of proflavine to the nitric oxide derivative of ferrous human adult hemoglobin (HbNO), the X-band EPR spectrum displays the characteristics which have been attributed to the T-state of the ligated tetramer. In parallel, oxygen affinity for the deoxygenated derivative of ferrous human adult Hb decreases in the presence of proflavine.

Coupling of the oxygen-linked interaction energy for inositol hexakisphosphate and bezafibrate binding to human HbA0.

The energetics of signal propagation between different functional domains (i.e. the binding sites for O2, inositol hexakisphospate (IHP), and bezafibrate (BZF)) of human HbA0 was analyzed at different heme ligation states and through the use of a stable, partially heme ligated intermediate.