The mechanism of reaction of nitrosyl with met- and oxymyoglobin: an ESR study.
In this ESR work we have studied the pentacoordinate symmetry in horse, whale and sperm-whale myoglobin (Mb) in different physical states such as solution and powder. Experiments were performed in which the following parameters were varied: the sample temperature, pH, reaction time with NO, and NO concentration. The results enabled us to explain the NO reaction mechanism in the oxy and met forms of myoglobin. The study of powder samples at different degrees of hydration allowed us to identify the diamagnetic intermediate species existent in the reaction of NO with met-Mb proposed in the literature. The results presented explain adequately the pH effect and temperature dependence observed in the ESR spectra obtained using the met-Mb sample solutions from Sigma Chemical Co., which consist of a mixture (13%) of Mb-O2.
Neto
L M
LM
EMBRAPA-UAPDIA, São Carlos, Brasil.
Nascimento
O R
OR
Tabak
M
M
Caracelli
I
I
D004578:Electron Spin Resonance Spectroscopy; D006420:Hemeproteins; D008786:Metmyoglobin; D009211:Myoglobin; D009609:Nitrous Oxide
D006420:Hemeproteins; D009211:Myoglobin; C017595:oxymyoglobin; D008786:Metmyoglobin; D009609:Nitrous Oxide