Effect of cobalt complexes on zinc finger peptide structure we examined the peptide by cd spectropolarimetry to verify that the peptide adopts a zinc finger structure in solution in the absence of zinc, the peptide displays a spectrum characteristic of typical random coil structure with an intense negative band below 200 nm. Working in zinc: kinetic investigations of a new zinc catalyst (see scheme) for the copolymerization of co 2 and epoxides show a reversible shift in the rate-determining step from epoxide ring opening to co 2 insertion, depending on the applied pressure this shift is attributed to the similarity of the activation barriers and explains the exceptionally high activities for the copolymerization.
Cobalt complexes containing tetradentate phosphine ligands with pendant proton relays were found to be active electrocatalysts for the production of hydrogen the h−co read more bond energetics of potential intermediates were explored by experiment and computation. Various effects have been identified, including the displacement of zinc, eg, by cadmium or cobalt, the formation of mixed complexes, incomplete coordination of toxic metal ions, as well as the oxidation of cysteine residues within the metal-binding domain.
In contrast, complexes with substitutionally inert axial ligands, such as imidazole (im) or 4-methylimidazole (4-meim), are poor protein inhibitors in general, coordination behavior of cobalt schiff base complexes is dependent on the oxidation state of the metal ion.
Key message zat11, a zinc finger of arabidopsis thaliana 11, is a dual-function transcriptional regulator that positively regulates primary root growth but negatively regulates ni 2+ tolerance zat11, a zinc finger transcription factor, is a negative regulator of nickel ion tolerance in arabidopsis | springerlink. An experiment on the synthesis of zinc finger disruptors via cobalt complexes (1113 words, 6 pages) zinc finger disruptors have been synthesized in the path via cobalt complexes there has been success in finding complexes that can selectively inhibit zinc finger proteins and stop dna replication. Cobalt citrate complexes have also been used to study the distribution of cobalt within cobalt/alumina catalyst bodies cobalt complexes of multidentate ligands, by comparison, have only recently gained attention as mri contrast agents, but the early results in this field demonstrate the great potential of such systems, and the fact that cobalt complexes are uniquely placed to be report on their chemical environment.
Zinc finger structures are frequently found in transcription factors and dna repair proteins, mediating dna-protein and protein-protein binding as low concentrations of transition metal compounds, including those of cadmium, nickel, and cobalt, have been shown to interfere with dna transcription. Structural disruption of the zinc finger motif by [co(acacen)(l) 2)] + complexes the interaction of 1 with his residues is hypothesized to inhibit tfs via displacement of the tetrahedral zn ii ion with 1.
Zinc finger of arabidopsis thaliana 11 (zat11) is a c 2 h 2-type zinc finger protein that has been reported to function as an active transcriptional repressor however, the biological function of zat11 remains unknown.