title: The nature of the nitric oxide complexes of lipoxygenase.
abstract: The NO complex of lipoxygenase with EPR signals near g = 4.0 is an S = 3/2 system with D approximately 15 cm-1 similar to Fe2+-EDTA-NO. This may result from antiferromagnetic coupling of axial (D greater than E) high spin ferrous iron to NO. The other NO complex of lipoxygenase, with EPR signals below ge, may result from rhombic high spin ferrous iron coupled to NO with D greater than J. The quenching of both signals by a hydroperoxy derivative of linoleic acid probably represents replacement of NO by an oxygen ligand.
mesh_terms: D001665:Binding Sites; D004578:Electron Spin Resonance Spectroscopy; D007501:Iron; D008084:Lipoxygenase; D008433:Mathematics; D009569:Nitric Oxide; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D009569:Nitric Oxide; D007501:Iron; D008084:Lipoxygenase