title: A structural model for the high-valent intermediate Q of methane monooxygenase from broken-symmetry density functional and electrostatics calculations.
abstract: A combined broken-symmetry density functional and electrostatics approach has been used to construct a model for the high-valent diiron intermediate Q of methane monooxygenase. The presence of high-spin or intermediate spin iron centers gives rise to two structurally distinct spin-coupled states of the cluster for which calculated geometries, net spin populations, Heisenberg J values, Mössbauer isomer shifts, and quadrupole splittings are compared and contrasted with the available spectroscopic data.
authors: Department of Molecular Biology, The Scripps Research Institute, La Jolla California 92037, USA. tlovell@scripps.edu
authors: Timothy
authors: T
authors: Lovell
authors: Wen-Ge
authors: WG
authors: Han
authors: Tiqing
authors: T
authors: Liu
authors: Louis
authors: L
authors: Noodleman
mesh_terms: D001665:Binding Sites; D007501:Iron / Q000737:chemistry; D010105:Oxygenases / Q000737:chemistry*; D011487:Protein Conformation; D015204:Spectroscopy, Mossbauer; D055672:Static Electricity
chemical_list: D007501:Iron; D010105:Oxygenases; C021555:methane monooxygenase