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Biomedical subjects

N J Turro

Publications and source records attributed to N J Turro.

28 records · Page 2Linked to original sources
PubMed1991

Interaction of horse plasma gelsolin with the hydrophobic fluorescent probe 2-(N-methylanilino)naphthalene-6-sulfonic acid.

Addition of horse plasma gelsolin to solutions of the fluorescent probe 2-(N-methylanilino)naphthalene-6-sulfonic acid (MANS) results in both a considerable enhancement and blue-shift of the MANS emission, indicative of hydrophobic interaction between MANS and gelsolin. Titrations suggest each gelsolin to bind two to three molecules of MANS, with a dissociation constant for each site of 0.24 microM. The peptide bond circular dichroism of gelsolin is unaffected by interaction with MANS, and viscosity data indicate that MANS does not inhibit the effects of gelsolin on actin polymerization. Fluorescence polarization data confirm gelsolin to be a globular protein and thermal denaturation studies suggest a cooperative melting transition for plasma gelsolin near 46 degrees C.

Anilino Naphthalenesulfonates↗
PubMed1990

Ligand-dependent interaction of ruthenium(II) polypyridyl complexes with DNA probed by emission spectroscopy.

The nature of the interaction in buffered aqueous solution of several homo and heteroleptic ruthenium(II) polypyridyl complexes containing 2,2'-bipyridine (bpy), 2,2'-bipyrazine (bpz), 1,10-phenanthroline (phen), 4,7-diphenyl-1,10-phenanthroline (dip), 3,4,7,8-tetramethyl-1,10-phenanthroline (tmp), 1,4,5,8-tetraazaphenanthrene (tap), and 1,4,5,8,9,12-hexaazatriphenylene (hat) with calf thymus DNA and poly(dA-dT).poly(dA-dT) (pdAT) has been investigated by steady-state spectroscopy and emission lifetime measurements. Those complexes containing two or more tap/hat ligands photo-oxidize the guanine base upon binding to DNA with efficiencies that parallel their excited state redox potentials, but display "normal" behavior (increase of both the emission intensity and lifetime) when bound to pdAT. However Ru(tap)(hat)2+2 and Ru(hat)2+3 even photooxidize the adenine base of pdAT, so that their excited states are also quenched in the presence of either polynucleotide. The electron transfer quenching mechanism has been confirmed previously by detection of the monoreduced complex in laser flash photolysis experiments in the presence of mononucleotides. Most of the complexes investigated appear to bind to DNA, at least in part via intercalation, with affinities being dependent on the nature of the largest ligand (hat shows the highest ability in heteroleptic complexes). From lifetime quenching experiments, in the presence of moderate amounts of NaCl, surface binding does not appear to be a general mode for the complexes investigated, and it has been demonstrated unequivocally only for Ru(phen)2+3. In addition, the intercalation of complexes into DNA increases as the ionic strength of the medium decreases, the DNA/Ru ratio increases, or when water is partially replaced by glycerol.

2,2'-Dipyridyl↗
PubMed1988

Accelerated electron transfer between metal complexes mediated by DNA.

DNA-mediated long-range electron transfer from photoexcited 1,10-phenanthroline complexes of ruthenium, Ru(phen)2(3)+, to isostructural complexes of cobalt(III), rhodium(III), and chromium(III) bound along the helical strand. The efficiency of transfer depended upon binding mode and driving force. For a given donor-acceptor pair, surface-bound complexes showed greater rate enhancements than those that were intercalatively bound. Even in rigid glycerol at 253 K, the rates for donor-acceptor pairs bound to DNA remained enhanced. For the series of acceptors, the greatest enhancement in electron-transfer rate was found with chromium, the acceptor of intermediate driving force. The DNA polymer appears to provide an efficient intervening medium to couple donor and acceptor metal complexes for electron transfer.

Binding, Competitive↗
PubMed1983

Influence of nuclear spin on chemical reactions: Magnetic isotope and magnetic field effects (A Review).

The course of chemical reactions involving radical pairs may depend on occurrence and orientation of nuclear spins in the pairs. The influence of nuclear spins is maximized when the radical pairs are confined to a space that serves as a cage that allows a certain degree of independent diffusional and rotational motion of the partners of the pair but that also encourages reencounters of the partners within a period which allows the nuclear spins to operate on the odd electron spins of the pair. Under the proper conditions, the nuclear spins can induce intersystem crossing between triplet and singlet states of radical pairs. It is shown that this dependence of intersystem crossing on nuclear spin leads to a magnetic isotope effect on the chemistry of radical pairs which provides a means of separating isotopes on the basis of nuclear spins rather than nuclear masses and also leads to a magnetic field effect on the chemistry of radical pairs which provides a means of influencing the course of polymerization by the application of weak magnetic fields.

Journal Article↗
PubMed1982

Pressure dependence of pyrene excimer fluorescence in human erythrocyte membranes.

The intensity of pyrene excimer fluorescence in human erythrocyte membranes and in sonicated dispersions of the membrane lipid (liposomes) was examined as a function of pressure (1-2080 bar) and temperature (5-40 degrees C). Higher pressure or lower temperature decreased the excimer/monomer intensity ratios. A thermotropic transition was detected in both membranes and liposomes by plots of the logarithm of the excimer/monomer intensity ratio versus 1/K. The transition temperature of the membranes was 19-21 degrees C at 1 bar and 28-31 degrees C at 450 bar, a shift with pressure of approx. 20-22 K per kbar. Corresponding transition temperatures of the liposomes were 21 degrees C at 1 bar and 33 degrees C at 450 bar, a shift of approx. 27 K per kbar. The observed pressure dependence of the thermotropic transition temperature is similar to that reported for phospholipid bilayers and greatly exceeds that of protein conformation changes. In concert with the liposome studies the results provide direct evidence for a lipid transition in the erythrocyte membrane.

Erythrocyte Membrane↗