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Cover Illustration: Cytochrome P450_cam is a hemoprotein that catalyzes the stereospecific hydroxylation of camphor (cam) at the 5-exo position in Pseudomonas putida. Molecular dynamics simulations were undertaken on the ternary inactive complex P450_cam(cam)(CO) to explore the CO migration pathways, monitor the internal cavities of the protein, and localize the CO docking sites. Here the protein is viewed from the distal side of the heme. Helices are in yellow, the rest of the backbone and the heme in light gray, and camphor in dark gray. To materialize the ligand docking sites, CO molecules from all trajectories have been superposed on the structure and drawn as red hard spheres. Water molecules located inside the protein, within a distance of 16.5 Å from its center of mass, are colored in blue: dark blue for water that has entered from the bulk and cyan for crystallographic waters. It can be seen that the solvent is localized in the less-helical moiety of the protein opposite to the CO docking sites. This shows that water molecules did not follow the same paths as CO despite the similar size of the two molecules, indicating that the polarity of the ligand plays a predominant role in its migration within the protein. (See Mouawad et al. pp. 781-794.)