title: Cooperative ligand reorientations in cytochrome c3: a molecular dynamics simulation.
abstract: Molecular dynamics simulations of a tetraheme cytochrome c3 were performed to investigate dynamic aspects of the motion of the axial heme iron ligands. It was found that persistent transitions between alternate axial imidazole orientations of the histidine incorporated in the CXXCH heme binding sequence occurred via correlated motions. The correlated motions involved virtually all of the atoms comprising the polypeptide backbone of the heme binding sequence as well as the histidine imidazole side-chain.
authors.affiliation: Central Research and Development Department, E.I. DuPont de Nemours & Co., Inc., Wilmington, DE.
authors.forename: P C
authors.initials: PC
authors.lastname: Weber
authors.forename: J J
authors.initials: JJ
authors.lastname: Wendoloski
authors.forename: F R
authors.initials: FR
authors.lastname: Salemme
mesh_terms: D000595:Amino Acid Sequence; D003198:Computer Simulation; D003574:Cytochrome c Group / Q000737:chemistry*; D003901:Desulfovibrio / Q000201:enzymology; D006418:Heme / Q000737:chemistry; D006639:Histidine / Q000737:chemistry; D007093:Imidazoles / Q000737:chemistry; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D003574:Cytochrome c Group; D007093:Imidazoles; D008024:Ligands; D006418:Heme; D006639:Histidine; C017165:cytochrome c(3)