E.p.r. studies of photolysis of nitrosyl haemoglobin at low temperatures: effects of quaternary structure.
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.
el-Jaick
L J
LJ
CBPF/CNPq, Rio de Janeiro, Brasil.
Wajnberg
E
E
Linhares
M P
MP
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
D006454:Hemoglobins; C008657:nitrosyl hemoglobin