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Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a 5- or 6-coordinate Fe--NO heme complex. The H93G mutation replaces the proximal histidine of Mb with glycine, allowi...
One of the difficulties in preparing accurate ambient-temperature model complexes for heme proteins, particularly in the ferric state, has been the generation of mixed-ligand adducts: complexes with d...
In the sperm whale myoglobin mutant H93G, the proximal histidine is replaced by glycine, leaving a cavity in which exogenous imidazole can bind and ligate the heme iron (Barrick, D. (1994) Biochemistr...
When nitric oxide (NO) binds to heme proteins, it exerts a repulsive trans effect on the proximal ligand, resulting in weakening or rupture of the proximal ligand-iron bond. The general question of wh...
The functional morphology and evolution of the nasal cavity is poorly understood. The New World Leaf-nosed bats of the family Phyllostomidae are an excellent group of mammals in which to study the evo...
Electric field produced inside a solute by a uniformly polarized liquid is strongly affected by dipolar polarization of the liquid at the interface. We show, by numerical simulations, that the electri...

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