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Biomedical subjects

J Peisach

Publications and source records attributed to J Peisach.

179 records · Page 10Linked to original sources
PubMed1970

Electron paramagnetic resonance study of the high- and low-spin forms of cytochrome P-450 in liver and in liver microsomes from a methylcholanthrene-treated rabbit.

The high- and low-spin forms of cytochrome P-450 were observed by electron paramagnetic resonance (epr) in a liver slice and in hepatic microsomes from a rabbit injected with methylcholanthrene. Quantitation of the epr absorption of these two chemical species and comparison with a preparation from a control rabbit showed that the single injection of drug increased the concentration of cytochrome P-450 to more than ten times its control value. Analysis of the epr spectrum for the high-spin compound showed that it is the most rhombically distorted ferric heme iron site yet observed (E/D = 0.10). It is suggested that microsomal cytochrome P-450 can exist in two interconvertible forms, in which the heme iron can either be high-spin or low-spin, depending upon the nature of the nonporphyrin ligands of the metal. There seems to be no need to postulate the existence of two different cytochrome P-450 proteins.

Adrenal Glands↗
PubMed1970

On the state of the iron and the nature of the ligand in oxyhemoglobin.

The structure of the oxygenated heme group of oxyhemoglobin may be formulated as [Hb(Heme d(1/2) (5)).OO(-)]. The heme iron atom is formally ferric, and the ligand is bound superoxide anion. When deoxyhemoglobin combines reversibly with oxygen a partial transfer of an electron occurs from the ferrous iron atom to the oxygen molecule. By surrendering its electron the iron atom has become ferric; in accepting an electron the ligated oxygen molecule has become a new species, the bound superoxide anion (.OO(-)). The configuration of the heme iron atom is deduced from comparison of the optical spectrum in the visible region of oxyhemoglobin with that of alkaline ferric hemoglobin whose configuration is established by electron paramagnetic resonance spectroscopy. The configuration of both species is low spin ferric heme iron (Heme d(1/2) (5)). The configuration of the ligated oxygen molecule of oxyhemoglobin is not accessible to study by magnetic or optical probes. However it may be known by analogy with the configuration of the ligated oxygen molecule of reversibly oxygenated cobalt complexes whose structure has been proved by both electron paramagnetic resonance and x-ray diffraction analysis. It is bound superoxide anion (.OO(-)). Other physical studies bearing on the structure of the oxygenated heme group are discussed. Reasons are given for believing that the proposed formulation of the oxyhemoglobin structure is consistent with the known stability of oxyhemoglobin.

Arteries↗
PubMed1969

Hemoglobin A: an electron paramagnetic resonance study of the effects of interchain contacts on the heme symmetry of high-spin and low-spin derivatives of ferric alpha chains.

Hemoglobin, the oxygen-binding heme protein of blood is composed of four subunits of two types, alpha and beta. Although the protein when isolated is diamagnetic, by oxidation it can be converted to various paramagnetic ferric forms exhibiting specific electron paramagnetic resonance (EPR) spectra. Using electron paramagnetic resonance, we have shown that the symmetry of the heme of isolated ferric alpha chains is different from that of the heme of these same subunits when associated with ferric beta chains in the parent tetramer. The high-spin form of the isolated ferric alpha chains shows a clearly resolved departure from tetragonal symmetry in contrast to ferrihemoglobin A, where the environment of the iron of all four chains is nearly tetragonal. This difference in heme symmetry suggests that the maintenance of tetragonal symmetry in the hemoglobin tetramer must be brought about by the configuration the alpha chains assume due to their contact with the beta chains. When isolated from the tetramer, some parts of the alpha chain must undergo physical displacement from a configuration that had been stabilized by the beta chains.Although differences in symmetry between monomer and tetramer are seen with high-spin forms, no such difference exists with two low-spin ferric forms. Here the symmetries of iron are primarily governed by the immediate ligand environment of the iron and not by the state of association of the protein.

Electron Spin Resonance Spectroscopy↗