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261.
Lactoperoxidase belongs to a family of mammalian peroxidases that catalyze the oxidation of halides and small organic molecules in the presence of H2O2. We have used photoacoustic calorimetry to characterize thermodynamic parameters associated with ligand dissociation from bovine milk lactoperoxidase. Upon CO photorelease, a prompt (tau < 50 ns) exothermic volume contraction (DeltaH = -20 +/- 7 kcal mol-1 and DeltaH = -2 +/- 1 mL mol-1) was measured at pH 7.0 and 4.0, whereas an endothermic expansion (DeltaH = 30 +/- 13 kcal mol-1 and DeltaV = 9 +/- 2 mL mol(-1)) was observed at pH 10.0 and 7.0 in the presence of 500 mM NaCl. We attribute the observed volume and enthalpy changes to electrostriction arising from changes in the charge distribution associated with a reorganization of the heme binding pocket upon ligand dissociation. It is likely that cleavage of the Fe-CO bond is accompanied by distortion of a salt bridge between Arg557 and the heme propionate group, resulting in the observed electrostriction due to changes in charge distribution. 相似文献
262.
B3LYP/6-31+G(d) and MP2/6-31+G(d) computations were performed on a series of ethynyl- and diethynyl-expanded tetrahedranes, prismanes, cubanes and adamantanes. Every ethynyl expansion reduces the ring strain energy of the cage. The deprotonation energies of the cage poly-ynes are exceptionally low; we estimate that the gas-phase deprotonation energy of the diethynyl-expanded cubane is about 309 kcal mol(-1). The ring and cage poly-ynes can serve as effective hosts of either lithium or sodium cation, where the best host maximizes the number of interactions of alkynyl groups with the cation at an ideal distance. Last, the vertical excitation energies of the poly-ynes and their conjugate bases suggest that the alkynyl groups are interacting through space. The poly-ynes express a broad range of absorption energies, indicating that these molecules are potential targets in expressly designed optical applications. 相似文献
263.
Sandra Bornemann Benjamin Rietschel Sabrina Baltruschat Michael Karas Bjoern Meyer 《Electrophoresis》2010,31(4):585-592
SDS‐PAGE is still one of the most widespread separation techniques in proteomic research and usually coupled to subsequent MS measurement for protein identification. The proteins are digested while embedded in the gel matrix. The resultant peptides are eluted out of the gel and finally analyzed. The in‐gel digestion process suffers from several drawbacks which influence the experimental outcome with respect to protein sequence coverage and detection sensitivity. Limited accessibility of the protease to the substrate protein and insufficient peptide extraction represent the two major problems. To specifically target these issues, we established a novel partly reversible gel system, in which the gel matrix can be conditionally cleaved to increase the pore diameters. By using a crosslinker mixture consisting of Bis and ethylene‐glycol‐diacrylate the acrylamide filament interconnections can be partly hydrolyzed in alkaline solution. The new hybrid gels have been tested to be compatible with a variety of acidic staining techniques. They exhibit similar electrophoretic performance compared with regular solely Bis‐based gels, but yield significantly better MS results. Thus, the Bis/ethylene‐glycol‐diacrylate SDS‐PAGE gel system is a promising alternative for MS‐based in‐gel workflows and might be transferred to other gel‐electrophoretic applications. 相似文献