title: Nitrosyl hemoglobin: EPR components at low temperatures.
abstract: The EPR spectrum of nitrosyl hemoglobin has been studied from 7.5 K to 104 K. It is composed of at least three components (A, B and C) which have a different dependence on temperature and power level. The A component decreases with increasing temperature. The B component disappears at around 30 K and is replaced by C. Relaxation of A follows the Orbach mechanism with an energy of 28 cm-1. This behavior can be attributed to phonon induced changes in the orientation of NO with respect to the heme plane.
authors.affiliation: CBPF/CNPq, Rio de Janeiro, Brasil.
authors.forename: E
authors.initials: E
authors.lastname: Wajnberg
authors.forename: M P
authors.initials: MP
authors.lastname: Linhares
authors.forename: L J
authors.initials: LJ
authors.lastname: el-Jaick
authors.forename: G
authors.initials: G
authors.lastname: Bemski
mesh_terms: D055592:Biophysical Phenomena; D001703:Biophysics; D004578:Electron Spin Resonance Spectroscopy; D006454:Hemoglobins; D006801:Humans; D008872:Microwaves; D013696:Temperature
chemical_list: D006454:Hemoglobins; C008657:nitrosyl hemoglobin