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FTIR and Resonance Raman Studies of Nitric Oxide Binding to H93G Cavity Mutants of Myoglobin
Animals Nitric Oxide Imidazoles Myoglobin Enzyme Inhibitors Free Radical Scavengers Spectroscopy, Fourier Transform Infrared Spectrum Analysis, Raman Binding Sites Molecular Structure
2016/5/23
Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a five- or six-coordinate Fe-NO complex. The H93G mutation eliminates the covalent attachment between the protein and ...
The Role of the Distal and Proximal Protein Environments in Controlling the Ferric Spin State and in Stabilizing Thiolate Ligation in Heme Systems:Thiolate Adducts of the Myoglobin H93G Cavity Mutant
salicylic alcohols hydrogen bonds quantum chemistry
2016/5/23
Recently, heme protein cavity mutants have been engineered in which the proximal coordinating amino acid has been replaced by a smaller, noncoordinating residue leaving a cavity that can be filled by ...
The efficiency of cavity sideband cooling of trapped molecules is theoretically investigated for the case where the IR transition between two rovibrational states is used as a cycling transition. The ...
A new quantum propagator for hard sphere and cavity systems
quantum propagator hard sphere cavity systems
2014/9/24
A new short time propagator for a particle interacting with a hard sphere or with a hard sphere cavity is derived. This new propagator is shown to be a much better approximation than the image approxi...