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Featured researches published by Robert S. Ehrlich.


Journal of Environmental Science and Health Part A-toxic\/hazardous Substances & Environmental Engineering | 1999

The relationship between adsorption of Cr(VI) and soil properties

Suen-Zone Lee; Lizone Chang; Robert S. Ehrlich

Abstract The adsorption of hexavalent chromium from dilute aqueous solution onto fifteen Taiwan soils has been investigated using pH as the major variable. The soil samples were thoroughly characterized for their physical chemical properties and composition of organic matter and metal oxides. The adsorption of Cr(VI) followed the Langmuir relation and decreased with increasing pH between pH 2.5 and 9.5. At constant pH and metal concentration, soils with greater organic matter content adsorbed more Cr(VI). The experimental results were tested in a partition coefficient model to relate the adsorption of the Cr (VI) by the different soils with soil components: organic matter, iron oxide, aluminum oxide and manganese oxide. This model was not successful when applied to measurements at the natural soil pH because of the competition of hydroxyl ions with hexavalent chromium for available sites. However, partition coefficients obtained from experimental dataat a fixed pH were highly correlated with those calcula...


Biochimica et Biophysica Acta | 1995

Cadmium-113 and magnesium-25 NMR study of the divalent metal binding sites of isocitrate dehydrogenases from pig heart.

Robert S. Ehrlich; Roberta F. Colman

The metal activator sites of NAD(+)-dependent and NADP(+)-dependent isocitrate dehydrogenases from pig heart have been probed using 113Cd- and 25Mg-NMR. In the presence of isocitrate and ADP, a broad resonance for cadmium bound to NAD-dependent isocitrate dehydrogenase was observed (-8 ppm) arising from exchange with isocitrate (-20 ppm) and/or ADP (27 ppm) complexes. The Cd shift with ADP suggests interaction of the metal with the nucleotide ring nitrogen. Increasing shifts with excess ADP are indicative of macrochelate formation. 25Mg-NMR demonstrates that, unlike manganese, magnesium has a similar dissociation constant (1.8 mM) from NADP-dependent isocitrate dehydrogenase as from the enzyme-isocitrate complex (1.1 mM). The extrapolated line width of bound magnesium increases from 674 Hz in the binary complex to 10,200 Hz in the ternary complex. The quadrupole coupling constant, calculated from relaxation rates, is larger in the ternary complex, indicative of greater distortion in the magnesium coordination sphere. The line widths of magnesium complexed to NAD-dependent isocitrate dehydrogenase are broader, as expected for the larger octamer. 113Cd- and 25Mg-NMR both show that the metal sites have anisotropic octahedral symmetry. 25Mg relaxation rates yield correlation times corresponding to motions of a domain with motion independent of the enzyme multimers.


Biochemistry | 1975

Coenzyme binding by native and chemically modified pig heart triphosphopyridine nucleotide dependent isocitrate dehydrogenase.

Robert S. Ehrlich; Roberta F. Colman


Journal of Biological Chemistry | 1981

Re-evaluation of molecular weight of pig heart NAD-specific isocitrate dehydrogenase.

Robert S. Ehrlich; Selma Hayman; Roberta F. Colman


Biochemistry | 1977

The role of arginine in the triphosphopyridine nucleotide dependent isocitrate dehydrogenase of pig heart.

Robert S. Ehrlich; Roberta F. Colman


Biochemistry | 1985

1H nuclear magnetic resonance studies of the conformation and environment of nucleotides bound to pig heart NADP+-dependent isocitrate dehydrogenase.

Robert S. Ehrlich; Roberta F. Colman


FEBS Journal | 1978

Histidine in the nucleotide-binding site of NADP-linked isocitrate dehydrogenase from pig heart.

Robert S. Ehrlich; Roberta F. Colman


Biochemistry | 1976

Influence of substrates and coenzymes on the role of manganous ion in reactions catalyzed by pig heart triphosphopyridine nucleotide-dependent isocitrate dehydrogenase

Robert S. Ehrlich; Roberta F. Colman


Biochemistry | 1990

Conformations of the coenzymes and the allosteric activator, ADP, bound to NAD(+)-dependent isocitrate dehydrogenase from pig heart.

Robert S. Ehrlich; Roberta F. Colman


Biochemistry | 1987

Ionization of isocitrate bound to pig heart NADP+-dependent isocitrate dehydrogenase: 13C NMR study of substrate binding.

Robert S. Ehrlich; Roberta F. Colman

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