title: The mechanism for the reversible oxygen addition to heme. A theoretical CASPT2 study.
abstract: By performing CASPT2 calculations, the lowest energy pathway for oxygen addition to an isolated heme center of a heme-protein is evaluated and found to be reversible (the oxyheme compound is just 14.9 kcal mol(-1) more stable than the deoxyheme + O(2) reactants, and the energy barriers to dissociation are even smaller).
authors.affiliation: Departament de Química Física, Facultat de Química and CERQT, Parc Científic, Universitat de Barcelona, Av. Diagonal 647, Barcelona 08028, Spain.
authors.forename: Jordi
authors.initials: J
authors.lastname: Ribas-Ariño
authors.forename: Juan J
authors.initials: JJ
authors.lastname: Novoa
mesh_terms: D001665:Binding Sites; D006418:Heme / Q000737:chemistry* / Q000378:metabolism; D008956:Models, Chemical; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D010100:Oxygen / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D009211:Myoglobin; C055547:deoxymyoglobin; D006418:Heme; D010100:Oxygen