title: High-spin Ni(II), a surprisingly good structural model for [NiFe] hydrogenase.
abstract: The first density functional calculations on high-spin (HS) Ni(II) models for the active site of the [NiFe] hydrogenases predict a ligand arrangement about Ni that is in better agreement with the crystal structures than previous predictions for low-spin (LS) Ni(II) models. With the crystal structures' geometry, the HS form is approximately 20 kcal/mol lower in energy than the LS one.
authors.affiliation: Department of Chemistry, Texas A&M University, TAMU 3255, College Station, Texas 77843-3255, USA.
authors.forename: Hua-Jun
authors.initials: HJ
authors.lastname: Fan
authors.forename: Michael B
authors.initials: MB
authors.lastname: Hall
mesh_terms: D001665:Binding Sites; D003901:Desulfovibrio / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009532:Nickel / Q000737:chemistry*; D009942:Organometallic Compounds / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D009942:Organometallic Compounds; D009532:Nickel; C043296:nickel-iron hydrogenase; D006864:Hydrogenase