title: First- and second-sphere contributions to Fe(II) site activation by cosubstrate binding in non-heme Fe enzymes.
abstract: Non-heme Fe(II) enzymes exhibit a general mechanistic strategy where binding all cosubstrates opens a coordination site on the Fe(II) for O2 activation. This study shows that strong-donor ligands, steric interactions with the substrate and second-sphere H-bonding to the facial triad carboxylate allow for five-coordinate site formation in this enzyme superfamily.
authors.affiliation: Department of Chemistry, Stanford University, Stanford, USA. Edward.solomon@stanford.edu.
authors.forename: Kenneth M
authors.initials: KM
authors.lastname: Light
authors.forename: John A
authors.initials: JA
authors.lastname: Hangasky
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Knapp
authors.forename: Edward I
authors.initials: EI
authors.lastname: Solomon
mesh_terms: D004798:Enzymes / Q000737:chemistry*; D005296:Ferrous Compounds / Q000737:chemistry*; D006418:Heme / Q000737:chemistry; D013379:Substrate Specificity
chemical_list: D004798:Enzymes; D005296:Ferrous Compounds; D006418:Heme