Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins.
The Q-band (35 GHz) electron paramagnetic resonance (EPR) spectra of nitrosyl hemoglobin (HbNO) and nitrosyl myoglobin (MbNO) were studied as a function of temperature between 19 K and 200 K. The spectra of both heme proteins show two classes of variations as a function of temperature. The first one has previously been associated with the existence of two paramagnetic species, one with rhombic and the other with axial symmetry. The second one manifests itself in changes in the g-factors and linewidths of each species. These changes are correlated with the conformational substates model and associate the variations of g-values with changes in the angle of the N(his)-Fe-N(NO) bond in the rhombic species and with changes in the distance between Fe and N of the proximal (F8) histidine in the axial species.
Flores
M
M
Centro Brasileiro de Pesquisas Fisicas, Rio de Janeiro, Brazil.
Wajnberg
E
E
Bemski
G
G
D055592:Biophysical Phenomena; D001703:Biophysics; D004578:Electron Spin Resonance Spectroscopy; D006442:Glycated Hemoglobin / Q000737:chemistry*; D006420:Hemeproteins / Q000737:chemistry*; D006801:Humans; D009211:Myoglobin / Q000031:analogs & derivatives* / Q000737:chemistry; D009569:Nitric Oxide / Q000737:chemistry*; D013696:Temperature; D013816:Thermodynamics
D006442:Glycated Hemoglobin; D006420:Hemeproteins; D009211:Myoglobin; D009569:Nitric Oxide; C058377:hemoglobin A, glycosylated-nitric oxide complex; C031560:myoglobin nitroxide