title: E.p.r. studies of photolysis of nitrosyl haemoglobin at low temperatures: effects of quaternary structure.
abstract: Photolysis of nitrosyl haemoglobin (HbNO) has been studied from 6.5 K to 20 K for different NO saturation conditions. The kinetic curves are fitted equally well by a biphasic exponential and a distribution of activation energies. The parameters are straightforwardly related to the quaternary structure of the protein. The biphasic model indicates that two germinate processes in the NO reassociation to Hb dominate at low temperatures independent of the protein conformation.
authors.affiliation: CBPF/CNPq, Rio de Janeiro, Brasil.
authors.forename: L J
authors.initials: LJ
authors.lastname: el-Jaick
authors.forename: E
authors.initials: E
authors.lastname: Wajnberg
authors.forename: M P
authors.initials: MP
authors.lastname: Linhares
mesh_terms: D003080:Cold Temperature; D004578:Electron Spin Resonance Spectroscopy; D006454:Hemoglobins / Q000737:chemistry* / Q000528:radiation effects; D006801:Humans; D007700:Kinetics; D015394:Molecular Structure; D009010:Monte Carlo Method; D010782:Photolysis; D011487:Protein Conformation
chemical_list: D006454:Hemoglobins; C008657:nitrosyl hemoglobin