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Biomedical subjects

M J Stillman

Publications and source records attributed to M J Stillman.

At least 55 records · Page 3Linked to original sources
PubMed1984

Temperature dependence in the absorption spectra of beef liver catalase.

The spin characteristics of the ferric heme groups in native beef liver catalase, and in the complexes formed by reaction with fluoride, cyanide, azide, thiocyanate, and cyanate ions have been studied using absorption spectroscopy over the temperature range of 4-285 K. The azide, isothiocyanate, and isocyanate complexes of catalase are considered to be high-spin ferric heme complexes at room temperature, but undergo a thermal spin change below 300 K. The temperature dependence of these absorption spectra, however, cannot be analyzed in terms of simple Boltzmann distributions between two S = 1/2 and S = 5/2 spin states. The data show that these spin changes occur over a very narrow temperature range, but do not result in the formation of completely, low-spin complexes. The data also suggest that the thermal spin changes that occur below the glassing temperature of the solvent are dependent upon the conformational changes which take place within the protein itself with a change in temperature, and which directly affect the environment of the heme group.

Animals↗
PubMed1983

Spectroscopic characterization of rat kidney Hg,Cu-metallothionein.

Absorption, circular dichroism (CD), magnetic circular dichroism (MCD) and emission spectra are reported for rat kidney Hg,Cu-metallothionein isoform 3 isolated following induction of the metallothionein with HgCl2. While the absorption spectrum is featureless, both the CD and MCD spectra show resolved bands that arise from the Cu-thiolate and Hg-thiolate groups. The emission spectrum at 77 K is much more complicated than would be expected for a copper (I)-containing metallothionein. It is suggested the emission only arises from the copper-thiolate groups but that the presence of the mercury results in copper ions in several different environments depending on the nature of the nearest neighbour.

Animals↗
PubMed1983

The temperature dependence of the MCD spectrum of horseradish peroxidase compound I.

The magnetic circular dichroism spectrum of the compound I species of horseradish peroxidase, which contains an iron (IV) porphyrin pi-cation radical complex, has been measured between 273 K and 4.2 K. The spectrum is temperature independent between 273 K and 30 K. However, very strong temperature dependence is observed below 30 K. These data do not appear to fit the temperature dependence expected for the presence of a simple MCD C term, or combination of C terms, but suggest that an increase in the coupling between the S = 1 iron (IV), and the S = 1/2 porphyrin pi-cation radical occurs forming a degenerate ground state. This increase in coupling below 30 K may be the result of a phase change in the protein which in turn affects the electronic structure of the heme group.

Chemical Phenomena↗
PubMed1981

Evidence for heme pi cation radical species in compound I of horseradish peroxidase and catalase.

Magnetic circular dichroism spectra are reported for the compound I species of beef liver catalase (hydrogen-peroxide: hydrogen-peroxide oxidoreductase, EC 1.11.1.6) and horseradish peroxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7) and the pi cation radical derivatives of porphyrins that have been suggested as models of the electronic configuration of the heme in the compound I species of these enzymes. Comparison of the magnetic circular dichroism spectra of the compound I species with the spectra of [Co(octaethylporphyrin)]2Br and [Co(octaethylporphyrin)]2ClO4 indicates that in both the intermediate enzyme species the heme has been oxidized to a pi cation radical. While there is a clear distinction between the magnetic circular dichroism spectra of the 2A2u porphyrin [Co(III)octaethylporphyrin]2ClO4, and the 2A1u porphyrin, [Co(III)octaethylporphyrin]2Br, such specific differences are not observed in the spectra of the two enzymes. Analysis of our data suggests that the ground states in the two enzymes are far more similar than the ground states in the two model porphyrins.

Animals↗
PubMed1980

Magnetic circular dichroism studies on the electronic configuration of catalase compounds I and II.

Absorption and magnetic circular dichroism spectra of native catalase, compound I and compound II have been measured and the data compared with that observed previously for horseradish peroxidase. The native catalase data at pH 6.9 are characteristic of a high-spin ferric porphyrin and are similar to the data reported for the ferric myoglobin and ferric horseradish peroxidase at pH 7. Oxidation of native catalase by peroxoacetic acid forms the compound I species that is identified by its low absorbance in the 400 nm Soret region and a series of overlapping bands between 450 nm and 680 nm. The magnetic circular dichroism spectra of compound I of catalase closely resembles that previously obtained for horseradish peroxidase compound I. These results indicate that the ground state of the heme pi-system is the same in both catalase and horseradish peroxidase compound I species. The compound II data show that the ratio of the magnetic circular dichroism intensity for the Soret to alpha A terms is 0.5 which means that there is a redistribution of angular momentum between the pi* excited states that give rise to the Soret and alpha-bands compared with the horseradish peroxidase compound II data where the ratio of the analogous A term intensities has a value of about 3. In addition, the magnetic CD spectra of both the catalase and horseradish peroxidase compound II species are reminiscent of typical metalloporphyrin spectra which lack charge-transfer transitions and where the metal d-orbitals are decoupled from the porphyrin pi-system.

Animals↗
PubMed1979

Magnetic circular dichroism studies of bovine liver catalase.

Absorption, circular dichroism (CD) and magnetic circular dichroism (MCD) spectra of beef liver catalase at pH 5.0 and 6.9, and its complexes with NaF, KCNO, NaCNS, NaN3 and NaCN, have been measured between 250 nm and 700 nm at room temperature. The pH 6.9 native catalase MCD shows the presence of several additional transitions not resolved in the absorption spectrum. While these bands can be seen in the spectra of all the derivatives, with the exception of the cyanide, their relative intensities changes considerably between complexes. Of special interest in the MCD of ferric hemes is the signal intensity at about 400 nm and 620 nm. The data indicate that the MCD intensity at 620 nm increases as the high spin iron porphyrin fraction increases, reaching a maximum with the fluoride complex. The 430 nm band intensity increases as the proportion of low spin iron increases, reaching a maximum with the cyanide complex. The MCD spectra also indicate clearly the existence of spin mixtures in the complexes with CNO-, CNS-, and N3-, where both the 430 nm and 620 nm bands have appreciable intensity. It is significant that despite almost identical absorption spectra the CNS- complex has higher fraction of low spin iron than either the CNO- or the N3- species. The differences between the pH 5 and 6.9 MCD spectra of the native catalase suggest that the environment of the heme centre is sensitive to protonation.

Animals↗